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Food Additives (Hypochlorous Acid Water, Sodium Metabisulfite, and Sodium Sulfite) Strongly Affect the Chemical and Biological Properties of Vitamin B12 in Aqueous SolutionClick to copy article linkArticle link copied!
- Naho OkamotoNaho OkamotoThe United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori City, Tottori 680-8553, JapanMore by Naho Okamoto
- Tomohiro BitoTomohiro BitoThe United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori City, Tottori 680-8553, JapanFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Tomohiro Bito
- Nanami HiuraNanami HiuraFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Nanami Hiura
- Ayaka YamamotoAyaka YamamotoFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Ayaka Yamamoto
- Mayu IidaMayu IidaFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Mayu Iida
- Yasuhiro BabaYasuhiro BabaFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Yasuhiro Baba
- Tomoyuki FujitaTomoyuki FujitaFaculty of Agriculture, Department of Agricultural and Life Sciences, Shinshu University, Nagano 399-4598, JapanMore by Tomoyuki Fujita
- Atsushi IshiharaAtsushi IshiharaThe United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori City, Tottori 680-8553, JapanFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Atsushi Ishihara
- Yukinori YabutaYukinori YabutaThe United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori City, Tottori 680-8553, JapanFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Yukinori Yabuta
- Fumio Watanabe*Fumio Watanabe*Email: [email protected]. Tel/Fax: +81-857-31-5412.The United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori City, Tottori 680-8553, JapanFaculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, JapanMore by Fumio Watanabe
Abstract
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Food additives, such as hypochlorous acid water, sodium metabisulfite, and sodium sulfite, strongly affect the chemical and biological properties of vitamin B12 (cyanocobalamin) in aqueous solution. When cyanocobalamin (10 μmol/L) was treated with these compounds, hypochlorous acid water (an effective chlorine concentration of 30 ppm) rapidly reacted with cyanocobalamin. The maximum absorptions at 361 and 550 nm completely disappeared by 1 h, and vitamin B12 activity was lost. There were no significant changes observed in the absorption spectra of cyanocobalamin for 0.01% (w/v) sodium metabisulfite; however, a small amount of the reaction product was formed within 48 h, which was subsequently identified as sulfitocobalamin through high-performance liquid chromatography. Similar results were shown for sodium sulfite. The effects of these food additives on the vitamin B12 content of red shrimp and beef meats were determined, revealing no significant difference in vitamin B12 content of shrimp and beef meats with or without the treatment even in hypochlorous acid water. The results suggest that these food additives could not react with food vitamin B12 in food, as most of this vitamin present in food is its protein-bound form rather than the free form.
Copyright © 2020 American Chemical Society
Introduction
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Vitamin B12 or cobalamin (B12) is a well-established member of corrinoids. (1) B12 is synthesized by certain archaea and bacteria but not by animals or plants. (2) B12 synthesized by bacteria and archaea is accumulated in animal tissues through the natural food chain. (2) Thus, animal-derived foods are good sources of B12 for humans. (3,4) Consequently, strict vegetarians are at a greater risk of developing B12 deficiency. (5)
Following analysis of B12 compounds in various foods using liquid chromatography-tandem mass spectrometry, certain foods contained a substantial amount of pseudovitamin B12, (6−8) which has adenine in place of 5,6-dimethylbenzimidazole as base in the lower nucleotide of the molecule. (1) Moreover, an unnatural and inactive B12 compound, B12 [c-lactone], was found in some edible mushrooms. (9,10) B12 [c-lactone] was readily formed from B12 by treatment with the organochlorine antibacterial agent chloramine-T. (10) In addition, preliminary experiments indicate that B12 is completely inactivated upon treatment with hypochlorous acid water. Hypochlorous acid is usually used to sanitize food products such as vegetables, fruits, and meat. (11−13) This acid is widely used in the food industry as the disinfection agents of food processing equipment. (12,13) However, hypochlorous acid readily reacts with proteins to form an aggregate and oxidizes specific amino acids. (14,15) High hypochlorous acid treatment reportedly induces a significant decrease of vitamin C content in vegetables. (16) There is limited information on the disadvantages associated with the use of hypochlorous acid. If hypochlorous acid has the ability to readily degrade B12, ingestion of the formed products might induce B12 deficiency in humans. To study whether such B12 degradation products formed by hypochlorous acid are harmful to humans, some of these compounds, which were unstable, were purified and characterized in this study.
Furthermore, other preliminary experiments indicate that food additives such as sodium metabisulfite (15) and sodium sulfite (17,18) had the ability to change the ultraviolet-visible (UV–visible) absorption maxima of B12 in aqueous solution. These results and observations suggest the possibility that B12 is readily inactivated by treatment with these food additives; hence, its nutritional values may be significantly reduced.
In this study, we evaluated the effects of hypochlorous acid water, sodium metabisulfite, and sodium sulfite on the chemical and biological properties of B12 under aqueous conditions. Furthermore, we examined whether significant loss of B12 occurs in food treated with these food additives.
Materials and Methods
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Materials
Cyanocobalamin (CN-B12) and hydroxocobalamin were purchased from Sigma-Aldrich (St. Louis, MO). Sulfitocobalamin was synthesized from hydroxocobalamin by treatment with sodium sulfite according to the method described by Suarez-Moreira et al. (19) Food additives, such as hypochlorous acid water, sodium metabisulfite, and sodium sulfite were purchased from markets in Japan. Argentine red shrimp (Pleoticus muelleri [Bate]) was purchased from a local market in Tottori City, Japan.
UV-Visible Spectra of CN-B12 Treated with or without Food Additives in Aqueous Solution
Hypochlorous acid water was adjusted to an effective chlorine concentration of 30 ppm using an effective chlorine concentration measurement kit (AQ-102P; SIBATA Scientific Technology Ltd., Saitama, Japan). The other food additives (i.e., sodium metabisulfite and sodium sulfite) were dissolved in distilled water at a concentration of 0.01% (w/v). CN-B12 was dissolved in these food additive solutions at a final concentration of 10 μmol/L. These solutions were left for 0, 1, 24, and 48 h at room temperature (25 °C). At the indicated time points, the UV–visible absorption spectra of these solutions were measured using a UV–visible spectrophotometer (UV-2550; SHIMADZU Corp., Kyoto, Japan).
High-Performance Liquid Chromatography (HPLC) Analysis of B12 Compounds Formed by Treatment with These Food Additives
CN-B12 was treated with hypochlorous acid water (an effective chlorine concentration of 10 ppm) for 1 h as described above. Subsequently, the treated CN-B12 solution was immediately loaded onto a Sep-Pak Vac (5 g) C18 cartridge (Waters Corp., Milford, MA) equilibrated with 20 mL of distilled water after washing with 20 mL of 75% (v/v) ethanol solution. The C18 cartridge was washed with 20 mL of distilled water, and the B12 compounds were eluted with 75% (v/v) ethanol solution. The eluate was allowed to evaporate to dryness under reduced pressure, dissolved in a small amount of water, and subsequently used as a sample for HPLC analysis. The Shimadzu HPLC apparatus (SPD-10AV UV–Visible detector, SCL-10A VP system controller, DGU-20A3 degasser, LC-10Ai Pumps, CTO-6A column oven) and CDS ver. 5 chromato-data processing system (LAsoft, Ltd., Chiba, Japan) were used. An aliquot (30 μL) of the sample was placed on a reversed-phase HPLC column (Wakosil–II 5C18RS Φ 4.6 × 150 mm2; particle size 5 μm), which was equilibrated at 40 °C with 20% (v/v) methanol containing 1% (v/v) acetic acid at a flow rate of 1.0 mL/min. The B12 compounds were eluted for 20 min with a linear gradient of 20–90% (v/v) methanol solution containing 1% (v/v) acetic acid, followed by elution with 90% (v/v) methanol solution containing 1% (v/v) acetic acid for 10 min, and were monitored by measuring the absorbance at 361 nm. The B12 compounds were eluted as major six peaks with retention times of 8.6 (P-1), 10.9 (P-2), 12.3 (P-3), 14.7 (P-4), 15.9 (P-5), and 17.1 min (P-6). These peak fractions were collected and evaporated to dryness under reduced pressure and dissolved in a small amount of water. Each peak fraction was further purified using a reversed-phase HPLC under the same conditions. The B12 compounds P-2, P-3, and P-6 were homogeneously purified; however, we failed to purify the remaining B12 compounds owing to their instability.
CN-B12 was treated with sodium metabisulfite or sodium sulfite for 48 h as described above and immediately placed on a reversed-phase HPLC column (Wakosil–II 5C18RS Φ 4.6 × 150 mm2; particle size 5 μm), which was equilibrated at 40 °C with 20% (v/v) methanol containing 1% (v/v) acetic acid at a flow rate of 1.0 mL/min. The B12 compounds were isocratically eluted under the same conditions and monitored by measuring the absorbance at 361 nm.
B12-Dependent Escherichia coli 215 Bioautography of the B12 Compounds Formed by Hypochlorous Acid Water
Bioautography of B12 compounds was performed as previously described. (20) An aliquot (2 μL) of the partially purified sample (50 μg/L) using the Sep-Pak Vac (5 g) C18 cartridge as described above. The authentic CN-B12 (50 μg/L) were spotted on filter papers (circle; 8 mm), which were placed on 1.5% (w/v) agar containing a basal medium of E. coli 215 and incubated at 37 °C for approximately 20 h. The agar plate was sprayed with a methanol solution containing 2,3,5-triphenyltetrazolium salt to enable visualization of the B12 compounds, indicating E. coli growth.
Proton Nuclear Magnetic Resonance (1H NMR) Spectroscopy of the B12 Compounds Formed by Hypochlorous Acid Water
Purified B12 compounds with respective retention times of 10.9 (P-2), 12.3 (P-3), and 17.1 min (P-6) were analyzed using 1H NMR spectroscopy to characterize their chemical structures formed after treatment with hypochlorous acid water. NMR spectra were measured with a Bruker DRX500 (Bruker Daltonics, Billerica, MA). The spectra of compounds A–C were obtained in deuterium oxide at room temperature. Chemical shifts are given on a δ (ppm) scale with 3-(trimethylsilyl)propionic acid-d4 sodium salt (TSP) used as an internal standard.
Effect of These Food Additives on the B12 Content of Red Shrimp Meat
The edible portion (approximately 150 g) of Argentine red shrimps was collected and homogenized using a mortar and pestle. Subsequently, 1.0 mL of hypochlorous acid water (an effective chlorine concentration of 30 ppm), 0.1% (w/v) sodium metabisulfite solution, or 0.1% (w/v) sodium sulfite solution, and distilled water (control) were added to each 10 g of the shrimp meat homogenate, followed by thorough mixing. Three sets of putties (3 × 3 × 1 cm3) from each sample were formed and subsequently allowed to stand at 4 °C for 48 h in the dark. B12 was extracted from aliquots (2.0 g) of each stored sample and determined using Lactobacillus delbrueckii American Type Culture Collection (ATCC; Manassas, VA) 7830 bioassay as previously described. (21)
Effect of Various Concentrations of Hypochlorous Acid Water on the B12 Content of Beef Meat
Ground beef meat was treated with 1.0 mL of hypochlorous acid water (effective chlorine concentrations of 30, 60, and 80 ppm), followed by thorough mixing. Three sets of putties (3 × 3 × 1 cm3) from each beef meat were formed and subsequently allowed to stand at 4 °C for 48 h in the dark. B12 was extracted and assayed as described above.
Statistical Analysis
One-way analysis of variance and post-hoc analysis were performed using Dunnett’s multiple comparison tests to evaluate the effect of food additives on the B12 content of red shrimp meat and to determine the effect of various concentrations of hypochlorous acid water on the B12 content of ground beef meat. Analyses were performed using GraphPad Prism 3 for Windows version 2.01 (GraphPad Software Inc., La Jolla, CA). Data are presented as the mean ± standard error of the mean (SEM). p < 0.05 denoted statistically significant differences.
Results
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UV–Visible Spectra of CN-B12 Treated with or without Selected Food Additives in an Aqueous Solution
On the basis of preliminary experiments, hypochlorous acid water, sodium metabisulfite, and sodium sulfite were selected as food additives. Changes in the UV–visible spectra of CN-B12 after treatment with these food additives were monitored for 48 h to determine the degree of reaction in aqueous solution. The UV–visible absorption spectrum of a reaction mixture containing CN-B12 and hypochlorous acid water (an effective chlorine concentration of 30 ppm) showed that the absorption peak at 278 nm, which is the specific wavelength of CN-B12, disappeared from 0 h. Other specific absorption peaks at 361 and 550 nm were also shifted to 365 and to 586 nm, respectively, and thereafter were significantly decreased (Figure 1A). These specific absorption maxima of CN-B12 completely disappeared by 1 h.
Figure 1
Figure 1. UV–visible absorption spectra of CN-B12 after treatment with these food additives. CN-B12 was dissolved in hypochlorous acid water (at an effective chlorine concentration of 30 ppm) (A), 0.01% (w/v) sodium metabisulfite (B), and 0.01% (w/v) solution sodium sulfite (C) solutions at a final concentration of 10 μmol/L. These solutions were left for 0 h (—), 1 h (− − −), 24 h (- - -), and 48 h (······) at room temperature (25 °C). A solution of CN-B12 treated without these food additives was used as control (—). At the indicated time points, the UV–visible absorption spectra of these solutions were measured using a UV–visible spectrophotometer. These are typical spectrophotometric data obtained from three independent experiments.
Addition of 0.01% (w/v) sodium metabisulfite indicated that the specific absorption peaks at 278 and 361 nm were slightly increased and thereafter decreased during the time course; however, these specific absorption maxima of CN-B12 were hardly changed for 48 h (Figure 1B). Sodium sulfite also showed similar spectroscopic behavior (Figure 1C).
B12 Compounds Formed during Treatment with Hypochlorous Acid Water
The B12 compounds formed after treatment with these compounds were analyzed using HPLC to determine the effects of these food additives on the chemical structure and biological activity of CN-B12. When CN-B12 treated with hypochlorous acid water for 60 min was analyzed using a reversed-phase HPLC, there were no peaks observed with retention times of 7.2 and 7.7 min, which are derived from authentic CN-B12 and B12 [c-lactone], respectively. Instead, the B12 compounds were eluted as major six peaks with respective retention times of 8.6 (P-1), 10.9 (P-2), 12.3 (P-3), 14.7 (P-4), 15.9 (P-5), and 17.1 min (P-6) (Figure 2). The compounds P-2, P-3, and P-6 could be purified and subjected to 1H NMR spectroscopy.
Figure 2
Figure 2. HPLC patterns of the B12 compounds treated with hypochlorous acid water. CN-B12 was dissolved in hypochlorous acid water (at an effective chlorine concentration of 10 ppm) at a final concentration of 10 μmol/L and left for 1 h at room temperature (25 °C) in the dark. The CN-B12 solution was loaded onto a Sep-Pak Vac (5 g) C18 cartridge to remove the hypochlorous acid. The fraction of the B12 compounds was dissolved in a small amount of water and subsequently used as a sample for HPLC analysis. An aliquot (30 μL) of the sample was placed on a reversed-phase HPLC column. The B12 compounds were eluted for 20 min with a linear gradient of 20–90% (v/v) methanol solution containing 1% (v/v) acetic acid, followed by elution with 90% (v/v) methanol solution containing 1% (v/v) acetic acid for 10 min, and were monitored by measuring the absorbance at 361 nm. The HPLC patterns of the B12 compounds are typical data obtained from three independent experiments.
We compared the 1H NMR spectra of the purified compounds with that of authentic CN-B12 (Figure 3). In the spectrum of compound P-2 (Figure 4A), the signal corresponding to the olefinic proton at C10 disappeared, whereas the characteristic signals coupled with each other at δH 3.86 (1H, d, J = 19.0 Hz) and δH 3.15 (1H, d, J = 19.0 Hz) appeared. Thus, the carbon at this position may have been saturated by the treatment. The signal corresponding to R1 (δH 6.39) indicated the presence of a ribose group. Furthermore, signals corresponding to methyl groups B10, B11, and Pr3 were also detected, indicating the presence of dimethylbenzimidazole and β-aminoisopropyl groups. All of the remaining methyl groups (C53, C35, C25, C36, C54, C47, C46, and C20) on the corrin ring appeared at chemical shifts similar to authentic vitamin B12.
Figure 3
Figure 3. 1H NMR spectrum of authentic CN-B12.
Figure 4
Figure 4. 1H NMR spectra of B12 compounds formed during treatment with hypochlorous acid water. (A), Compound P-2 (with a retention time of 10.9 min); (B), compound P-3 (with a retention time of 12.3 min); and (C) compound P-6 (with a retention time of 17.1 min).
The spectra of compounds P-2 and P-3 (Figures 4A,B) were very similar to each other; however, the values of the chemical shift of the signals were different. The signals corresponding to B2, B4, B7, and R1 indicated the presence of dimethylbenzimidazole and a ribose group. All methyl groups corresponding to B12 were detected in the spectrum, indicating that the corrin ring skeleton and β-aminoisopropyl groups were retained in compound P-3. Therefore, compounds P-2 and P-3 may be structural isomers.
The signal corresponding to B4 at δH 7.32 remained on the dimethylbenzimidazole ring in the spectrum of compound P-6 (Figure 4C), whereas the signal corresponding to B7 disappeared. Thus, the B7 position on the dimethylbenzimidazole group was likely substituted by treatment. The chemical shifts of the signals of methyl groups at C35 and C53 (δH 2.62 and 2.61 ppm) showed high-magnetic field shifts. Additionally, the signal corresponding to the methyl group at C20 disappeared. Thus, the conjugation system of the corrin ring was modified by treatment.
B12 Compounds Formed during Treatment with Sodium Metabisulfite and Sodium Sulfite
Following the treatment of CN-B12 with sodium metabisulfite for 48 h and analysis using reversed-phase HPLC, the B12 compounds were isocratically eluted as major and minor peaks with retention times of 8.7 and 27.5 min, respectively (Figure 5A).
Figure 5
Figure 5. HPLC patterns of the B12 compounds treated with 0.01% (w/v) sodium metabisulfite. CN-B12 was dissolved in 0.01% (w/v) sodium metabisulfite solution at a final concentration of 10 μmol/L and left for 48 h at room temperature (25 °C) in the dark. (A) Treated CN-B12 solution (50 μL) or (B) authentic sulfitocobalamin (20 μL of 130 mg/L) was loaded onto a reversed-phase HPLC column. The B12 compounds were isocratically eluted and monitored by measuring the absorbance at 361 nm. Data are typical HPLC patterns of the B12 compounds treated with sodium metabisulfite or authentic sulfitocobalamin obtained from three independent experiments.
The major peak with a retention time of 8.7 min was identical to that of authentic CN-B12 (data not shown), suggesting that most CN-B12 was not changed by treatment with sodium metabisulfite. Previous studies reported that hydroxocobalamin was readily converted to sulfitocobalamin by the addition of sodium sulfite. (19,22) When sulfitocobalamin was prepared and analyzed using HPLC, the minor peak with a retention time of 27.5 min was identical to that of sulfitocobalamin (Figure 5B). Similar results were obtained for sodium sulfite (data not shown).
Biological Activity of the B12 Compounds Formed during Treatment with Selected Food Additives
Sulfitocobalamin is well established as a naturally occurring biologically active B12. (23) The minor peak (with a retention time of 27.5 min) formed by the addition of sodium metabisulfite or sodium sulfite (Figure 5A) was active in B12-dependent E. coli 215 (data not shown). However, based on the absence of bacterial growth, B12-dependent E. coli 215 bioautography of hypochlorous acid-treated B12 compounds indicated that hypochlorous acid water readily inactivated CN-B12 in aqueous solution (Figure 6).
Figure 6
Figure 6. Effects of the B12 compounds treated with hypochlorous acid water on B12-dependent E. coli 215. (A) Authentic B12 (100 pg) and (B) hypochlorous acid-treated B12 compounds after purification using a Sep-Pak Vac (5 g) C18 cartridge.
Effect of the Selected Food Additives on the B12 Content of Red Shrimp Meat
In Japan, sodium metabisulfite and sodium sulfite are typically used to prevent black discoloration in shrimps. Hypochlorous acid water (an effective chlorine concentration of 30 ppm), 0.1% (w/v) sodium metabisulfite solution, 0.1% (w/v) sodium sulfite solution, and distilled water (control) were added to red shrimp meats and then stored for 48 h at 4 °C in the dark to determine whether these food additives can reduce the B12 content in food. B12 was extracted from the red shrimp meat treated with or without these food additives, and its amount was determined using the L. delbrueckii ATCC 7830 bioassay. To evaluate the effect of food additives on the B12 content of red shrimp meat, one-way analysis of variance and post-hoc analysis were performed using Dunnett’s multiple comparison tests. When p < 0.05 denoted statistically significant differences, there was no significant decrease detected in the B12 content of the red shrimp meat treated with these food additives (Figure 7).
Figure 7
Figure 7. Effects of treatment with hypochlorous acid water, sodium metabisulfite, and sodium sulfite on the B12 content of red shrimp meat. The edible portion of Argentine red shrimps was collected and homogenized using a mortar and pestle. The shrimp meat homogenate (10 g) was treated with 1.0 mL of distilled water as a control (1), hypochlorous acid water (at an effective chlorine concentration of 30 ppm) (2), 0.1% (w/v) sodium metabisulfite solution (3), and 0.1% (w/v) sodium sulfite solution (4) and subsequently mixed. Three sets of putties (3 × 3 × 1 cm3) from each sample were formed and then allowed to stand at 4 °C for 48 h in the dark. The B12 was extracted from each stored sample, and its amount was determined using L. delbrueckii ATCC 7830 bioassay. B12 content was assayed in triplicate. Data are represented as means ± SEM (n = 3).
Effect of Various Concentrations of Hypochlorous Acid Water on the B12 Content of Ground Beef Meat
Hypochlorous acid is usually used to sanitize vegetables, fruits, and meat. (11−13) As animal-derived foods are good sources of B12 for humans, (3,4) the effect of various concentrations of hypochlorous acid on the B12 content of beef meat was evaluated. Effective chlorine concentrations of 30, 60, and 80 ppm of hypochlorous acid water and distilled water (control) were added to ground beef meats and then stored for 48 h at 4 °C in the dark. B12 was extracted from the ground beef meat treated with or without hypochlorous acid water, and its amount was determined using the bioassay. The B12 content of the ground beef meat gradually decreased with increased effective chlorine concentrations of hypochlorous acid, but there was no significant difference among these values (Figure 8).
Figure 8
Figure 8. Effects of various concentrations of hypochlorous acid water on the B12 content of ground beef meat. Ground beef meat (10 g) was treated with 1.0 mL of distilled water as a control (1) and treated with 1.0 mL of hypochlorous acid water at effective chlorine concentrations of 30 ppm (2), 60 ppm (3), and 80 ppm (4) and subsequently mixed. Three sets of putties (3 × 3 × 1 cm3) from each sample were formed and then allowed to stand at 4 °C for 48 h in the dark. B12 was extracted from each stored sample, and its amount was determined using L. delbrueckii ATCC 7830 bioassay. B12 content was assayed in triplicate. Data are represented as means ± SEM (n = 3).
Discussion
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An unnatural and inactive B12 compound, B12 [c-lactone], has been formed from B12 and the organochlorine antibacterial agent chloramine T. (10) Thus, food additives that may inactivate B12 were screened for their ability to change the UV–visible absorption spectra of CN-B12. According to the results of these preliminary experiments, hypochlorous acid water, sodium metabisulfite, and sodium sulfite were selected. Hypochlorous acid water is a highly safe antimicrobial agent and widely used as a food additive. (11−13) However, treatment with hypochlorous acid water (an effective chlorine concentration of 30 ppm) resulted in immediate and significant decreases of the absorption peaks at 278, 365, and 586 nm. Notably, these absorption maxima of CN-B12 completely disappeared by 1 h (Figure 1A). This finding suggested the destruction of the corrin ring and the liberation of the central cobalt ion of CN-B12 following treatment with hypochlorous acid water. A high concentration of hypochlorous acid reportedly induced the oxidative cleavage of the corrin ring and the porphyrin ring, destroying these compounds. (24,25) Although these observations suggest that the treatment of food with hypochlorous acid water induces significant loss of B12, this agent did not affect the level of B12 in this study (Figures 7 and 8). These results imply that hypochlorous acid water could not react with food B12, which is present in its protein-bound form in food. (26,27) Hypochlorous acid is generated by myeloperoxidase and plays an important role in the innate immune system of mammals. (28) Nevertheless, it was suggested that highly generated hypochlorous acid leads to various diseases due to the action of a potent oxidant protein and induces chlorination and protein aggregation. (25,29) This observation suggests that hypochlorous acid water as a food additive adversely affects food proteins in foods, but not B12.
Through HPLC analysis, we detected five major peaks as degradation products from B12 by HPLC analysis. Among them, we analyzed three compounds eluted from the HPLC column at 10.9 (P-2), 12.3 (P-3), and 17.1 min (P-6), respectively, using 1H NMR spectroscopy. On the basis of the 1H NMR spectra, compounds P-2 and P-3 may be structural isomers, which lacked the olefinic proton at C10. On the other hand, compound P-6 lacked the B7 proton on the dimethybenzoimidazole ring instead of C10. Thus, the C10 position in the corrin ring appears to be the first site of reaction with hypochlorous acid water. Compound P-6 appears to be largely affected by treatment with hypochlorous acid water versus compared to compounds P-2 and P-3. These degradation products have not been detected in the oxidation process of B12. Determination of the chemical structures of these compounds would lead to a better understanding of the degradation mechanism of B12 by hypochlorous acid water.
When CN-B12 was treated with sodium metabisulfite or sodium sulfite for 48 h, a small amount of sulfitocobalamin was formed. Sulfitocobalamin was formed from glutathionylcobalamin, a product formed by the decyanation reaction of CN-B12 in the presence of reduced glutathione in mammalian cells. (30,31) Sulfitocobalamin, which is one of the naturally occurring cobalamins in foods, is biologically active in humans. However, it has been reported that, in humans, the intestinal absorption of sulfitocobalamin was lower than that of CN-B12. (23)
The results of this study indicate that these food additives have the ability to significantly change the properties of B12 in aqueous solution; however, they are unable to reduce the B12 content of food.
Author Information
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- Fumio Watanabe - The United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori City, Tottori 680-8553, Japan; Faculty of Agriculture, School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori 680-8553, Japan;
http://orcid.org/0000-0001-6654-4148;
N.O., A.Y., M.I., and Y.B. performed most experiments. T.F. and A.I. analyzed the cobalamin products formed by the addition of hypochlorous acid using 1H NMR spectroscopy and interpreted the results. N.O., T.B., Y.Y., A.I., and F.W. designed the experiments, interpreted the results, and wrote the manuscript. All authors commented on the manuscript and approved the final version.
Acknowledgments
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This work was supported by the JSPS KAKENHI Grant Numbers 16K07736 (F.W.).
References
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This article references 31 other publications.
- 1Watanabe, F.; Bito, T. Corrinoids in Food and Biological Samples, In Frontiers in Natural Product Chemistry, Atta-ur-Rahman, F. R. S., Eds.; Bentham Science, 2016; Vol. 2, pp 229– 244.Google ScholarThere is no corresponding record for this reference.
- 2Watanabe, F.; Bito, T. Vitamin B12 sources and microbial interaction. Exp. Biol. Med. 2018, 243, 148– 158, DOI: 10.1177/1535370217746612Google Scholar2Vitamin B12 sources and microbial interactionWatanabe, Fumio; Bito, TomohiroExperimental Biology and Medicine (London, United Kingdom) (2018), 243 (2), 148-158CODEN: EBMMBE; ISSN:1535-3699. (Sage Publications Ltd.)Vitamin B12 is synthesized only by certain bacteria and archaeon, but not by plants. The synthesized vitamin B12 is transferred and accumulates in animal tissues, which can occur in certain plant and mushroom species through microbial interaction. In particular, the meat and milk of herbivorous ruminant animals (e.g. cattle and sheep) are good sources of vitamin B12 for humans. Ruminants acquire vitamin B12, which is considered an essential nutrient, through a symbiotic relationship with the bacteria present in their stomachs. In aquatic environments, most phytoplankton acquire vitamin B12 through a symbiotic relationship with bacteria, and they become food for larval fish and bivalves. Edible plants and mushrooms rarely contain a considerable amt. of vitamin B12, mainly due to concomitant bacteria in soil and/or their aerial surfaces. Thus, humans acquire vitamin B12 formed by microbial interaction via mainly ruminants and fish (or shellfish) as food sources. In this review, up-to-date information on vitamin B12 sources and bioavailability are also discussed. To prevent vitamin B12 (B12) deficiency in high-risk populations such as vegetarians and elderly subjects, it is necessary to identify foods that contain high levels of B12. B12 is synthesized by only certain bacteria and archaeon, but not by plants or animals. The synthesized B12 is transferred and accumulated in animal tissues, even in certain plant tissues via microbial interaction. Meats and milks of herbivorous ruminant animals are good sources of B12 for humans. Ruminants acquire the essential B12 through a symbiotic relationship with bacteria inside the body. Thus, we also depend on B12-producing bacteria located in ruminant stomachs. While edible plants and mushrooms rarely contain a considerable amt. of B12, mainly due to concomitant bacteria in soil and/or their aerial surfaces. In this mini-review, we described up-to-date information on B12 sources and bioavailability with ref. to the interaction of microbes as B12-producers.
- 3Watanabe, F. Vitamin B12 sources and bioavailability. Exp. Biol. Med. 2007, 232, 1266– 1274, DOI: 10.3181/0703-MR-67Google Scholar3Vitamin B12 sources and bioavailabilityWatanabe, FumioExperimental Biology and Medicine (Maywood, NJ, United States) (2007), 232 (10), 1266-1274CODEN: EBMMBE; ISSN:1535-3702. (Society for Experimental Biology and Medicine)A review. The usual dietary sources of vitamin B12 are animal foods, meat, milk, egg, fish, and shellfish. As the intrinsic factor-mediated intestinal absorption system is estd. to be satd. at about 1.5-2.0 μg per meal under physiol. conditions, vitamin B12 bioavailability significantly decreases with increasing intake of vitamin B12 per meal. The bioavailability of vitamin B12 in healthy humans from fish meat, sheep meat, and chicken meat averaged 42%, 56%-89%, and 61%-66%, resp. Vitamin B12 in eggs seems to be poorly absorbed (<9%) relative to other animal food products. In the Dietary Ref. Intakes in the United States and Japan, it is assumed that 50% of dietary vitamin B12 is absorbed by healthy adults with normal gastrointestinal function. Some plant foods, dried green and purple lavers (nori) contain substantial amts. of vitamin B12, although other edible algae contained none or only traces of vitamin B12. Most of the edible blue-green algae (cyanobacteria) used for human supplements predominately contain pseudovitamin B12, which is inactive in humans. The edible cyanobacteria are not suitable for use as vitamin B12 sources, esp. in vegans. Fortified breakfast cereals are a particularly valuable source of vitamin B12 for vegans and elderly people. Prodn. of some vitamin B12-enriched vegetables is also being devised.
- 4Bito, T.; Watanabe, F.; Tanioka, Y. Characterization of vitamin B12 compounds from marine foods. Fish. Sci. 2018, 84, 747– 755, DOI: 10.1007/s12562-018-1222-5Google Scholar4Characterization of vitamin B12 compounds from marine foodsBito, Tomohiro; Tanioka, Yuri; Watanabe, FumioFisheries Science (Tokyo, Japan) (2018), 84 (5), 747-755CODEN: FSCIEH; ISSN:0919-9268. (Springer Japan)A review. Vitamin B12 is synthesized by only certain bacteria and archaea but not by animals or plants. In marine environments, bacterial vitamin B12 is transferred and concd. into fish and shellfish bodies by plankton in the marine food chain. Moreover, marine macrophytic red algae, Porphyra spp. specifically contain substantial amts. of vitamin B12, due to microbial interaction. Although some meats or viscera of edible fish and shellfish are excellent sources of biol. active vitamin B12, an inactive corrinoid, pseudovitamin B12, was found in some edible shellfish using liq. chromatog./electrospray ionization-tandem mass spectrometry. To prevent elderly people from developing vitamin B12 deficiency due to food protein-bound vitamin B12 malabsorption, we present a survey of marine foods contg. free vitamin B12. The results of our study suggest that bonito and clam exts. (or soup stocks), which contain considerable amts. of free vitamin B12 are useful not only as seasonings and flavorings but also as excellent sources of free vitamin B12.
- 5Watanabe, F.; Yabuta, Y.; Tanioka, Y.; Bito, T. Biologically active vitamin B12 compounds in foods for preventing deficiency among vegetarians and elderly subjects. J. Agric. Food Chem. 2013, 61, 6769– 6775, DOI: 10.1021/jf401545zGoogle Scholar5Biologically Active Vitamin B12 Compounds in Foods for Preventing Deficiency among Vegetarians and Elderly SubjectsWatanabe, Fumio; Yabuta, Yukinori; Tanioka, Yuri; Bito, TomohiroJournal of Agricultural and Food Chemistry (2013), 61 (28), 6769-6775CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)A review. The usual dietary sources of vitamin B12 are animal-source based foods, including meat, milk, eggs, fish, and shellfish, although a few plant-based foods such as certain types of dried lavers (nori) and mushrooms contain substantial and considerable amts. of vitamin B12, resp. Unexpectedly, detailed characterization of vitamin B12 compds. in foods reveals the presence of various corrinoids that are inactive in humans. The majority of edible blue-green algae (cyanobacteria) and certain edible shellfish predominately contain an inactive corrinoid known as pseudovitamin B12. Various factors affect the bioactivity of vitamin B12 in foods. For example, vitamin B12 is partially degraded and loses its biol. activity during cooking and storage of foods. The intrinsic factor-mediated gastrointestinal absorption system in humans has evolved to selectively absorb active vitamin B12 from naturally occurring vitamin B12 compds., including its degrdn. products and inactive corrinoids that are present in daily meal foods. The objective of this review is to present up-to-date information on various factors that can affect the bioactivity of vitamin B12 in foods. To prevent vitamin B12 deficiency in high-risk populations such as vegetarians and elderly subjects, it is necessary to identify plant-source foods that contain high levels of bioactive vitamin B12 and, in conjunction, to prep. the use of cryst. vitamin B12-fortified foods.
- 6Watanabe, F.; Katsura, H.; Takenaka, S.; Fujita, T.; Abe, K.; Tamura, Y.; Nakatsuka, T.; Nakano, Y. Pseudovitamin B12 is the predominant cobamide of an algal health food, Spirulina Tablets. J. Agric. Food Chem. 1999, 47, 4736– 4741, DOI: 10.1021/jf990541bGoogle Scholar6Pseudovitamin B12 Is the Predominant Cobamide of an Algal Health Food, Spirulina TabletsWatanabe, Fumio; Katsura, Hiromi; Takenaka, Shigeo; Fujita, Tomoyuki; Abe, Katsuo; Tamura, Yoshiyuki; Nakatsuka, Toshiyuki; Nakano, YoshihisaJournal of Agricultural and Food Chemistry (1999), 47 (11), 4736-4741CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)The vitamin B12 concn. of an algal health food, Spirulina (Spirulina sp.) tablets, was detd. by both Lactobacillus leichmannii ATCC 7830 microbiol. and intrinsic factor chemiluminescence methods. The values detd. with the microbiol. method were ∼6-9-fold greater in the Spirulina tablets than the values detd. with the chemiluminescence method. Although most of the vitamin B12 detd. with the microbiol. method was derived from various vitamin B12 substitutive compds. and/or inactive vitamin B12 analogs, the spirulina contained a small amt. of vitamin B12 active in the binding of the intrinsic factor. Two intrinsic factor active vitamin B12 analogs (major and minor) were purified from the spirulina tablets and partially characterized. The major (83%) and minor (17%) analogs were identified as pseudovitamin B12 and vitamin B12, resp., as judged from data of TLC, reversed-phase HPLC, 1H NMR spectroscopy, UV-visible spectroscopy, and biol. activity using L. leichmannii as a test organism and the binding of vitamin B12 to the intrinsic factor.
- 7Miyamoto, E.; Tanioka, Y.; Nakao, T.; Barla, F.; Inui, H.; Fujita, T.; Watanabe, F.; Nakano, Y. Purification and characterization of a corrinoid-compound in an edible cyanobacterium Aphanizomenon flos-aquae as a nutritional supplementary food. J. Agric. Food Chem. 2006, 54, 9604– 9607, DOI: 10.1021/jf062300rGoogle Scholar7Purification and characterization of a corrinoid compound in an edible Cyanobacterium Aphanizomenon flos-aquae as a nutritional supplementary foodMiyamoto, Emi; Tanioka, Yuri; Nakao, Tomoyuki; Barla, Florin; Inui, Hiroshi; Fujita, Tomoyuki; Watanabe, Fumio; Nakano, YoshihisaJournal of Agricultural and Food Chemistry (2006), 54 (25), 9604-9607CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)The vitamin B12 concn. of the dried cells of Aphanizomenon flos-aquae was detd. by both microbiol. method with Lactobacillus delbrueckii ATCC7830 and chemiluminescence method with intrinsic factor. The Aphanizomenon cells contained 616.3 ± 30.3 μg (n = 4) of vitamin B12 per 100 g of the dried cells by the microbiol. method. The values detd. with the chemiluminescence method, however, were only about 5.3% of the values detd. by the microbiol. method. A corrinoid compd. was purified from the dried cells and characterized. The purified corrinoid compd. was identified as pseudovitamin B12 (an inactive corrinoid compd. for humans) by silica gel 60 TLC, C18 reversed-phase HPLC, UV-visible spectroscopy, and 1H NMR spectroscopy. The results suggest that the Aphanizomenon cells are not suitable for use as a vitamin B12 source, esp. in vegans.
- 8Teng, F.; Tanioka, Y.; Hamaguchi, N.; Bito, T.; Takenaka, S.; Yabuta, Y.; Watanabe, F. Determination and characterization of vitamin B12 compounds in edible sea snails, ivory shell Babylonia japonica and turban shell Turdo Batillus cornutus. Fish. Sci. 2015, 81, 1105– 1111, DOI: 10.1007/s12562-015-0920-5Google Scholar8Determination and characterization of vitamin B12 compounds in edible sea snails, ivory shell Babylonia japonica and turban shell Turdo Batillus cornutusTeng, Fei; Tanioka, Yuri; Hamaguchi, Natsumi; Bito, Tomohiro; Takenaka, Shigeo; Yabuta, Yukinori; Watanabe, FumioFisheries Science (Tokyo, Japan) (2015), 81 (6), 1105-1111CODEN: FSCIEH; ISSN:0919-9268. (Springer Japan)In this study, we characterized and quantified vitamin B12 compds. in popular edible snails Babylonia japonica and Turdo Batillus cornutus using a microbiol. assay based on Lactobacillus delbrueckii subsp. lactis ATCC 7830. The meat and viscera of B. japonica contained 27.2 ± 9.1 and 92.8 ± 25.8 μg of vitamin B12 per 100 g, resp. However, the meat and viscera of T. cornutus contained extremely low amts. of vitamin B12 (3.0 ± 1.5 and 15.1 ± 8.3 μg of vitamin B12 per 100 g, resp.). We identified the vitamin B12 compds. from the edible portions (meat and viscera) of B. japonica and T. cornutus using liq. chromatog.-electrospray ionization/tandem mass spectrometry. We found that B. japonica contained substantial amts. of true vitamin B12, while pseudovitamin B12 was the predominant corrinoid in T. cornutus. These results indicate that the meat and viscera of B. japonica are excellent sources of vitamin B12 for humans.
- 9Bito, T.; Teng, F.; Ohishi, N.; Takenaka, S.; Miyamoto, E.; Sakuno, E.; Terashima, K.; Yabuta, Y.; Watanabe, F. Characterization of vitamin B12 compounds in the fruiting bodies of shiitake mushroom (Lentinura edodes) and bed logs after fruiting of the mushroom. Mycoscience 2014, 55, 462– 468, DOI: 10.1016/j.myc.2014.01.008Google Scholar9Characterization of vitamin B12 compounds in the fruiting bodies of shiitake mushroom (Lentinula edodes) and bed logs after fruiting of the mushroomBito, Tomohiro; Teng, Fei; Ohishi, Noriharu; Takenaka, Shigeo; Miyamoto, Emi; Sakuno, Emi; Terashima, Kazuhisa; Yabuta, Yukinori; Watanabe, FumioMycoscience (2014), 55 (6), 462-468CODEN: MNCEED; ISSN:1340-3540. (Elsevier Japan K. K.)This study detd. the vitamin B12 content in com. available dried fruiting bodies of shiitake mushroom, Lentinula edodes. The vitamin B12 contents in dried donko-type fruiting bodies with closed caps (5.61 ± 3.90 μg/100 g dry wt.), did not significantly differ from those of dried koushin-type fruiting bodies with open caps (4.23 ± 2.42 μg/100 g dry wt.). The bed logs after fruiting of the mushroom also contained the vitamin B12 levels similar to that in the dried shiitake fruiting bodies. To det. whether the dried shiitake fruiting bodies and their bed logs contained vitamin B12 or other corrinoid compds. that are inactive in humans, we purified corrinoid compds. using an immunoaffinity column and identified vitamin B12 using vitamin B12-dependent Escherichia coli 215 bioautograms and liq. chromatog.-electrospray ionization tandem mass spectrometry (LC/ESI-MS/MS) chromatograms. Dried shiitake fruiting bodies rarely contained an unnatural corrinoid vitamin B12[c-lactone] that is inactive in humans. Given that shiitake mushroom lacks the ability to synthesize vitamin B12de novo, the vitamin B12 found in dried shiitake fruiting bodies must have been derived from the bed logs.
- 10Teng, F.; Bito, T.; Takenaka, S.; Yabuta, Y.; Watanabe, F. Vitamin B12[c-lactone], a biologically inactive corrinoid compound, occurs in cultured and dried lion’s mane mushroom (Hericium erinaceus) fruiting bodies. J. Agric. Food Chem. 2014, 62, 1726– 1732, DOI: 10.1021/jf404463vGoogle Scholar10Vitamin B12[c-lactone], a Biologically Inactive Corrinoid Compound, Occurs in Cultured and Dried Lion's Mane Mushroom (Hericium erinaceus) Fruiting BodiesTeng, Fei; Bito, Tomohiro; Takenaka, Shigeo; Yabuta, Yukinori; Watanabe, FumioJournal of Agricultural and Food Chemistry (2014), 62 (7), 1726-1732CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)This study detd. the vitamin B12 content of the edible medicinal mushroom Hericium erinaceus, lion's mane mushroom fruiting body, using a microbiol. assay based on Lactobacillus delbrueckii ATCC 7830. Trace levels (0.04-0.36 μg/100 g dry wt.) of vitamin B12 were found in most of the dried mushroom samples, and two samples contained slightly higher levels (0.56 and 1.04 μg/100 g dry wt., resp.) of vitamin B12. We purified the corrinoid compds. from the exts. of dried lion's mane mushroom fruiting bodies using an immunoaffinity column and identified them as vitamin B12 or vitamin B12[c-lactone] (or both) based on LC/ESI-MS/MS chromatograms. This is the first report on an unnatural corrinoid, vitamin B12[c-lactone], occurring in foods. Vitamin B12[c-lactone] was simple to produce during incubation of authentic vitamin B12 and chloramine-T, an antimicrobial agent, at varying pH values (3.0-7.0) and was completely inactive in the vitamin B12-dependent bacteria that are generally used in vitamin B12 bioassays.
- 11Hakim, H.; Alam, M. S.; Sangsriratanakul, N.; Nakajima, K.; Kitazawa, M.; Ota, M.; Toyofuku, C.; Yamada, M.; Thammakarn, C.; Shoham, D.; Takehara, K. Inactivation of bacteria on surfaces by sprayed slightly acidic hypochlorous acid water: in vitro experiments. J. Vet. Med. Sci. 2016, 78, 1123– 1128, DOI: 10.1292/jvms.16-0075Google Scholar11Inactivation of bacteria on surfaces by sprayed slightly acidic hypochlorous acid water: in vitro experimentsHakim, Hakimullah; Alam, Md. Shahin; Sangsriratanakul, Natthanan; Nakajima, Katsuhiro; Kitazawa, Minori; Ota, Mari; Toyofuku, Chiharu; Yamada, Masashi; Thammakarn, Chanathip; Shoham, Dany; Takehara, KazuakiJournal of Veterinary Medical Science (2016), 78 (7), 1123-1128CODEN: JVMSEQ; ISSN:0916-7250. (Japanese Society of Veterinary Science)The capacity of slightly acidic hypochlorous acid water (SAHW), in both liq. and spray form, to inactivate bacteria was evaluated as a potential candidate for biosecurity enhancement in poultry prodn. SAHW (contg. 50 or 100 ppm chlorine, pH 6) was able to inactivate Escherichia coli and Salmonella Infantis in liq. to below detectable levels (≤2.6 log10 CFU/mL) within 5 s of exposure. In addn., SAHW antibacterial capacity was evaluated by spraying it using a nebulizer into a box contg. these bacteria, which were present on the surfaces of glass plates and rayon sheets. SAHW was able to inactivate both bacterial species on the glass plates (dry condition) and rayon sheets within 5 min spraying and 5 min contact times, with the exception of 50 ppm SAHW on the rayon sheets. Furthermore, a corrosivity test detd. that SAHW does not corrode metallic objects, even at the longest exposure times (83 days). Our findings demonstrate that SAHW is a good candidate for biosecurity enhancement in the poultry industry. Spraying it on the surfaces of objects, eggshells, egg incubators and transport cages could reduce the chances of contamination and disease transmission. These results augment previous findings demonstrating the competence of SAHW as an anti-viral disinfectant.
- 12Veasey, S.; Muriana, P. M. Evaluation of electrolytically-generated hypochlorous acid (‘Electrolyzed water’) for sanitation of meat and meat-contact surfaces. Foods 2016, 5, 42, DOI: 10.3390/foods5020042Google Scholar12Evaluation of electrolytically-generated hypochlorous acid ('electrolyzed water') for sanitation of meat and meat-contact surfacesVeasey, Shawnna; Muriana, Peter M.Foods (2016), 5 (2), 42/1-42/15CODEN: FOODBV; ISSN:2304-8158. (MDPI AG)'Electrolyzed water' generators are readily available in the food industry as a renewable source of hypochlorous acid that eliminates the need for workers to handle hazardous hypochlorite concs. We applied electrolyzed water (EW) directly to multi-strain cocktails of Listeria monocytogenes, E. coli O157:H7, and Salmonella sp. at 250 ppm free available chlorine (FAC) and achieved greater than 6-log redns. in 2 min. Lower EW values were examd. as antimicrobial interventions for fresh meat (beef carcasses), processed meats (frankfurters), and food contact surfaces (slicing blades). Little or no redn. relative to controls was obsd. when generic E. coli-inoculated beef carcasses or L. monocytogenes-inoculated frankfurters were showered with EW. Spray application of EW (25 and 250-ppm FAC) onto L. monocytogenes-inoculated slicing blades showed that greater redns. were obtained with 'clean' (3.6 and 5.7-log redn.) vs. 'dirty' (0.6 and 3.3-log redn.) slicing blades, resp. Trials with L. monocytogenes-inoculated protein-EW solns. demonstrated that protein content as low as 0.1% is capable of eliminating FAC, reducing antimicrobial activity against L. monocytogenes. EW appears better positioned as a surface sanitizer with minimal org. material that can otherwise act as an effective reducing agent to the oxidizing soln. rendering it ineffective.
- 13Quan, Y.; Kim, H.-Y.; Shin, I.-S. Bactericidal activity of strong acidic hypochlorous water against Escherichia coli O157:H7 and Listeria monocytogenes in biofilms attached to stainless steel. Food Sci. Biotechnol. 2017, 26, 841– 846, DOI: 10.1007/s10068-017-0086-2Google Scholar13Bactericidal activity of strong acidic hypochlorous water against Escherichia coli O157:H7 and Listeria monocytogenes in biofilms attached to stainless steelQuan, Yaru; Kim, Hee-Yeon; Shin, Il-ShikFood Science and Biotechnology (2017), 26 (3), 841-846CODEN: FSBOBR; ISSN:1226-7708. (Korean Society of Food Science and Technology)This study aims to investigate the bactericidal activity of strong acidic hypochlorous water (SAHW) against Escherichia coli O157:H7 and L. monocytogenes in bacterial biofilms. The bactericidal activity of SAHW against both bacteria in colony biofilm increased with the elevation of the available chlorine concn. (ACC) and extension of the treatment time. The survived cell counts of E. coli O157:H7 and L. monocytogenes in the biofilms were significantly (p < 0.05) decreased compare to tap water at more than 30 mg/L of ACC in SAHW and 15 s of treatment time. E. coli O157:H7 and L. monocytogenes in the biofilms reduced to less than the detection limit by treatment of 50 mg/L of ACC in SAHW for 300 and 600 s, resp. SAHW may be a potential disinfecting agent for removing bacterial biofilms from food processing equipment and other facilities.
- 14Pattison, D. I.; Davies, M. J. Absolute rate constants for the reaction of hypochlours acid with protein side chains and peptide bonds. Chem. Res. Toxicol. 2001, 14, 1453– 1464, DOI: 10.1021/tx0155451Google Scholar14Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bondsPattison, David I.; Davies, Michael J.Chemical Research in Toxicology (2001), 14 (10), 1453-1464CODEN: CRTOEC; ISSN:0893-228X. (American Chemical Society)Hypochlorous acid (HOCl) is a potent oxidant, which is produced in vivo by activated phagocytes. This compd. is an important antibacterial agent, but excessive or misplaced prodn. has been implicated in a no. of human diseases, including atherosclerosis, arthritis, and some cancers. Proteins are major targets for this oxidant, and such reaction results in side-chain modification, backbone fragmentation, and crosslinking. Despite a wealth of qual. data for such reactions, little abs. kinetic data is available to rationalize the in vitro and in vivo data. In this study, abs. second-order rate consts. for the reactions of HOCl with protein side chains, model compds., and backbone amide (peptide) bonds have been detd. at physiol. pH values. The reactivity of HOCl with potential reactive sites in proteins is summarized by the series: Met (3.8 × 107 M-1 s-1) > Cys (3.0 × 107 M-1 s-1) » cystine (1.6 × 105 M-1 s-1) ≈ His (1.0 × 105 M-1 s-1) ≈ α-amino (1.0 × 105 M-1 s-1) > Trp (1.1 × 104 M-1 s-1) > Lys (5.0 × 103 M-1 s-1) » Tyr (44 M-1 s-1) ≈ Arg (26 M-1 s-1) > backbone amides (10-10-3 M-1 s-1) > Gln (0.03 M-1 s-1) ≈ Asn (0.03 M-1 s-1). The rate consts. for reaction of HOCl with backbone amides (peptide bonds) vary by 4 orders of magnitude with uncharged peptide bonds reacting more readily with HOCl than those in a charged environment. These kinetic parameters have been used in computer modeling of the reactions of HOCl with human serum albumin, apolipoprotein-A1 and free amino acids in plasma at different molar excesses. These models are useful tools for predicting, and reconciling, exptl. data obtained in HOCl-induced oxidns. and allow estns. to be made as to the flux of HOCl to which proteins are exposed in vivo.
- 15Kerkaert, B.; Mestdagh, F.; Cucu, T.; Aedo, P. R.; Ling, S. Y.; De Meulenaer, B. Hypochlorous and peracetic acid induced oxidation of dairy proteins. J. Agric. Food Chem. 2011, 59, 907– 914, DOI: 10.1021/jf1037807Google Scholar15Hypochlorous and Peracetic Acid Induced Oxidation of Dairy ProteinsKerkaert, Barbara; Mestdagh, Frederic; Cucu, Tatiana; Aedo, Philip Roger; Ling, Shen Yan; De Meulenaer, BrunoJournal of Agricultural and Food Chemistry (2011), 59 (3), 907-914CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)Hypochlorous and peracetic acids, both known disinfectants in the food industry, were compared for their oxidative capacity toward dairy proteins. Whey proteins and caseins were oxidized under well controlled conditions at pH 8 as a function of the sanitizing concn. Different markers for protein oxidn. were monitored. The results established that the protein carbonyl content was a rather unspecific marker for protein oxidn., which did not allow one to differentiate the oxidant used esp. at the lower concns. Cysteine, tryptophan, and methionine were proven to be the most vulnerable amino acids for degrdn. upon hypochlorous and peracetic acid treatment, while tyrosine was only prone to degrdn. in the presence of hypochlorous acid. Hypochlorous acid induced oxidn. gave rise to protein aggregation, while during peracetic acid induced oxidn., no high mol. wt. aggregates were obsd. Protein aggregation upon hypochlorous acid oxidn. could primarily be linked to tryptophan and tyrosine degrdn.
- 16Vandekinderen, I.; Van Camp, J.; Devlieghere, F.; Veramme, K.; Bernaert, N.; Denon, Q.; Ragaert, P.; De Meulenaer, B. Effect of decontamination on the microbial load, the sensory quality and the nutrient retention of ready-to-eat white cabbage. Eur. Food Res. Technol. 2009, 229, 443– 455, DOI: 10.1007/s00217-009-1069-1Google Scholar16Effect of decontamination on the microbial load, the sensory quality and the nutrient retention of ready-to-eat white cabbageVandekinderen, Isabelle; Camp, John; Devlieghere, Frank; Veramme, Kim; Bernaert, Nathalie; Denon, Quenten; Ragaert, Peter; Meulenaer, BrunoEuropean Food Research and Technology (2009), 229 (3), 443-455CODEN: EFRTFO; ISSN:1438-2377. (Springer GmbH)The effect of different decontamination treatments such as washing with sodium hypochlorite (20 and 200 mg/L), peroxyacetic acid (80 and 250 mg/L), neutral electrolyzed oxidizing water (4.9 and 31.7 mg/L free chlorine) and contact with 1.55 mg/L chlorine dioxide gas on the microbial and sensory quality, and the nutrient content of fresh-cut white cabbage was studied. Only rinsing with 200 mg/L sodium hypochlorite, peroxyacetic acid or contact with gaseous chlorine dioxide resulted in significantly higher redns. of the total plate count (1.5-2.5 log cfu/g) than the ones achieved by washing with tap water (0.5 log cfu/g). However, those treatments giving the best results from a microbial point of view induced significant changes in the sensory quality. Regarding the effects on nutrient content, the mech. effects caused by water washing already reduced the vitamin C content by 16-29%. Contrary to washing with neutral electrolyzed oxidizing water and contact with chlorine dioxide gas, a supplementary decrease of the vitamin C content ranging between 9 and 28% was obsd., when peroxyacetic acid or 200 mg/L sodium hypochlorite were used. After the use of peroxyacetic acid or gaseous chlorine dioxide, the phenol content also showed a decreasing trend, although not statistically significant. Apart from the effect of washing with water, the lipophilic nutrients were well retained after a decontamination step except for the α-tocopherol content, when peroxyacetic acid was used (-43 to 56%), and for the all-trans-β-carotene content (-8%) of cabbage in contact with gaseous chlorine dioxide. Because of its potential to reduce the initial microbial load without neg. effects on the sensory quality, in combination with its limited effects on nutrient content, a treatment with 80 mg/L peroxyacetic acid is preferable to decontaminate fresh-cut white cabbage.
- 17Ahmadi, F.; Lee, Y. H.; Lee, W. H.; Oh, Y. K.; Park, K. K.; Kwak, W. S. Preservation of fruit and vegetable discards with sodium metabisulfite. J. Envrion. Manage. 2018, 224, 113– 121, DOI: 10.1016/j.jenvman.2018.07.044Google ScholarThere is no corresponding record for this reference.
- 18Luo, X.-Y.; Tu, Y.-G.; Zhao, Y.; Li, J.-K.; Wang, J.-J. Effects of sulfhydryl compounds, carbohydrates, organic acids, and sodium sulfite on the formation of lysinoalamine in preserved egg. J. Food Sci. 2014, 79, 1621– 1629, DOI: 10.1111/1750-3841.12543Google Scholar18Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved EggLuo, Xu-ying; Tu, Yong-gang; Zhao, Yan; Li, Jian-ke; Wang, Jun-jieJournal of Food Science (2014), 79 (8), T1621-T1628CODEN: JFDSAZ; ISSN:0022-1147. (Wiley-Blackwell)To identify inhibitors for lysinoalanine formation in preserved egg, sulfhydryl compds. (glutathione, L-cysteine), carbohydrates (sucrose, D-glucose, maltose), org. acids (L-ascorbic acid, citric acid, DL-malic acid, lactic acid), and sodium sulfite were individually added at different concns. to a pickling soln. to prep. preserved eggs. Lysinoalanine formation as an index of these 10 substances was detd. Results indicate that glutathione, D-glucose, maltose, L-ascorbic acid, citric acid, lactic acid, and sodium sulfite all effectively diminished lysinoalanine formation in preserved egg albumen and yolk. When 40 and 80 mmol/L of sodium sulfite, citric acid, L-ascorbic acid, and D-glucose were individually added into the pickling soln., the inhibition rates of lysinoalanine in the produced preserved egg albumen and yolk were higher. However, the attempt of minimizing lysinoalanine formation was combined with the premise of ensuring preserved eggs quality. Moreover, the addn. of 40 and 80 mmol/L of sodium sulfite, 40 and 80 mmol/L of D-glucose, 40 mmol/L of citric acid, and 40 mmol/L of L-ascorbic acid was optimal to produce preserved eggs. The corresponding inhibition rates of lysinoalanine in the albumen were approx. 76.3% to 76.5%, 67.6% to 67.8%, 74.6%, and 74.6%, and the corresponding inhibition rates of lysinoalanine in the yolk were about 68.7% to 69.7%, 50.6% to 51.8%, 70.4%, and 57.8%. It was concluded that sodium sulfite, D-glucose, L-ascorbic, and citric acid at suitable concns. can be used to control the formation of lysinoalanine during preserved egg processing. Achieved results may be helpful to select several food ingredients or additives effective in inhibiting the toxic component lysinoalanine formation during preserved egg processing. Furthermore, it is geared toward building a lysinoalanine control system, and providing a theor. ref. for the processing of preserved egg.
- 19Suarez-Moreira, E.; Hannibal, L.; Smith, C. A.; Chavez, R. A.; Jacobsen, D. W.; Brasch, N. E. A simple, convenient method to synthesize cobalamins: synthesis of homocysteinylcobalamin, N-acetylcysteinylcobalamin, 2-N-acetylamino-2-carbomethoxyethanethiolatocobalamin, sulfitocobalamin and nitorocobalamin. Dalton Trans. 2006, 28, 5269– 5277, DOI: 10.1039/b610158eGoogle ScholarThere is no corresponding record for this reference.
- 20Tanioka, Y.; Yabuta, Y.; Miyamoto, E.; Inui, H.; Watanabe, F. Analysis of vitamin B12 in food by silica gel 60 TLC and bioautography with vitamin B12-dependent Escherichia coli 215. J. Liq. Chromatogr. Relat. Technol. 2008, 31, 1977– 1985, DOI: 10.1080/10826070802197453Google Scholar20Analysis of Vitamin B12 in Food by Silica Gel 60 TLC and Bioautography with Vitamin B12-Dependent Escherichia coli 215Tanioka, Yuri; Yabuta, Yukinori; Miyamoto, Emi; Inui, Hiroshi; Watanabe, FumioJournal of Liquid Chromatography & Related Technologies (2008), 31 (13), 1977-1985CODEN: JLCTFC; ISSN:1082-6076. (Taylor & Francis, Inc.)To evaluate whether certain foods contain vitamin B12 or inactive corrinoids, a simple technique, bioautog. with vitamin B12-dependent Escherichia coli mutant after sepn. of the sample by silica gel 60 thin-layer chromatog., is available. By using the method, vitamin B12-compds. found in some edible cyanobacteria are readily identified. This bioautog. has great advantages (simplicity, speed, and inexpensiveness) for the anal. of vitamin B12-compds. in food.
- 21Watanabe, F.; Bito, T. Determination of cobalamin and related compounds in foods. J. AOAC Int. 2018, 101, 1308– 1313, DOI: 10.5740/jaoacint.18-0045Google Scholar21Determination of cobalamin and related compounds in foodsWatanabe, Fumio; Bito, TomohiroJournal of AOAC International (2018), 101 (5), 1308-1313CODEN: JAINEE; ISSN:1060-3271. (AOAC International)Cobalamin, also known as the red-colored vitamin B12, is found in animal-based foods such as meat, milk, and fish. Various cobalamin compds. are extd. from foods and converted into cyanocobalamin, which is most stable, to be analyzed by various methods. Traditionally, the cobalamin content of foods is detd. by microbiol. assay with Lactobacillus delbrueckii subsp. lactis American Type Culture Collection 7830. However, this lactic acid bacterium can substitute deoxyribosides or deoxynucleotides (known as an alkali-resistant factor) for cobalamin. Therefore, cobalamin contents detd. by this microbiol. assay are often incorrect in some foods. The difficulty of evaluating whether certain foods contain cobalamin or inactive corrinoids (or both) may be easily resolved by the use of bioautog. with a cobalamin-dependent Escherichia coli after sepn. of the sample by silica gel TLC. LC/electrospray ionization-tandem mass spectrometry is also used to analyze corrinoid compds., and various inactive corrinoid compds. have been identified in foods.
- 22Derevenkov, I. A.; Salnikov, D. S.; Makarov, S. V.; Boss, G. R.; Koifman, O. I. Kinetics and mechanism of oxidation of super-reduced cobalamin and cobinamide by thiosulfate, sulfite and dithionite. Dalton Trans. 2013, 42, 15307– 15316, DOI: 10.1039/c3dt51714dGoogle ScholarThere is no corresponding record for this reference.
- 23Farquharson, J.; Adams, J. F. The forms of vitamin B12 in foods. Br. J. Nutr. 1976, 36, 127– 136, DOI: 10.1079/BJN19760063Google Scholar23The forms of vitamin B12 in foodsFarquharson, J.; Adams, J. F.British Journal of Nutrition (1976), 36 (1), 127-36CODEN: BJNUAV; ISSN:0007-1145.Vitamin B12 in the forms of sulfitocobalamin [15671-27-9], hydrocobalamin [13422-51-0], methylcobalamin [13422-55-4], cyanocobalamin [68-19-9], and adenosylcobalamin [13870-90-1] was detected in 23 items of food prepd. for consumption. Intestinal absorption of sulfitocobalamin was lower than that of cyanocobalamin in 9 subjects.
- 24Abu-Soud, H. M.; Maitra, D.; Byun, J.; Souza, C. E. A.; Banejee, J.; Saed, G. M.; Diamond, M. P.; Andreana, P. R.; Pennathur, S. The reaction of HOCl and cyanocobalamin: Corrin destruction and the liberation of cyanogen chloride. Free Radical Biol. Med. 2012, 52, 616– 625, DOI: 10.1016/j.freeradbiomed.2011.10.496Google Scholar24The reaction of HOCl and cyanocobalamin: Corrin destruction and the liberation of cyanogen chlorideAbu-Soud, Husam M.; Maitra, Dhiman; Byun, Jaeman; Souza, Carlos Eduardo A.; Banerjee, Jashoman; Saed, Ghassan M.; Diamond, Michael P.; Andreana, Peter R.; Pennathur, SubramaniamFree Radical Biology & Medicine (2012), 52 (3), 616-625CODEN: FRBMEH; ISSN:0891-5849. (Elsevier B.V.)Overprodn. of hypochlorous acid (HOCl) has been assocd. with the development of a variety of disorders such as inflammation, heart disease, pulmonary fibrosis, and cancer through its ability to modify various biomols. HOCl is a potent oxidant generated by the myeloperoxidase-hydrogen peroxide-chloride system. Recently, we have provided evidence to support the important link between higher levels of HOCl and heme destruction and free iron release from Hb and RBCs. Our current findings extend this work and show the ability of HOCl to mediate the destruction of metal-ion derivs. of tetrapyrrole macrocyclic rings, such as cyanocobalamin (Cobl), a common pharmacol. form of vitamin B12. Cyanocobalamin is a water-sol. vitamin that plays an essential role as an enzyme cofactor and antioxidant, modulating nucleic acid metab. and gene regulation. It is widely used as a therapeutic agent and supplement, because of its efficacy and stability. In this report, we demonstrate that although Cobl can be an excellent antioxidant, exposure to high levels of HOCl can overcome the beneficial effects of Cobl and generate proinflammatory reaction products. Our rapid kinetic, HPLC, and mass spectrometric analyses showed that HOCl can mediate corrin ring destruction and liberate cyanogen chloride (CNCl) through a mechanism that initially involves α-axial ligand replacement in Cobl to form a chlorinated deriv., hydrolysis, and cleavage of the phosphonucleotide moiety. Addnl., it can liberate free Co, which can perpetuate metal-ion-induced oxidant stress. Taken together, these results are the first report of the generation of toxic mol. products through the interaction of Cobl with HOCl.
- 25Maita, D.; Byun, J.; Andreana, P. R.; Abdulhamid, I.; Saed, G. M.; Diamond, M. P.; Pennathur, S.; Abu-Soud, H. M. Mechanism of hypochlorous acid-mediated heme destruction and free iron release. Free Radical Biol. Med. 2011, 51, 364– 373, DOI: 10.1016/j.freeradbiomed.2011.03.040Google ScholarThere is no corresponding record for this reference.
- 26Teng, F.; Bito, T.; Takenaka, S.; Yabuta, Y.; Watanabe, F. Yoke of the century egg (Pidan) contains a readily digestible form of free vitamin B12. J. Nutr. Sci. Vitaminol. 2016, 62, 366– 371, DOI: 10.3177/jnsv.62.366Google Scholar26Yolk of the century egg (pidan) contains a readily digestible form of free vitamin B12Teng, Fei; Bito, Tomohiro; Takenaka, Shigeo; Yabuta, Yukinori; Watanabe, FumioJournal of Nutritional Science and Vitaminology (2016), 62 (5), 366-371CODEN: JNSVA5; ISSN:0301-4800. (Center for Academic Publications Japan)In this study, we detd. the vitamin B12 content of com. available century eggs (pidan) and characterized their vitamin B12 compns. in detail. The egg yolk and white of century eggs (each 100 g wet wt.) contained 1.9 ± 0.6 and 0.8 ± 0.3 μg of vitamin B12, resp. The vitamin B12 compds. purified from the egg yolk and white were identified as vitamin B12 using liq. chromatog.-electrospray ionization/tandem mass spectrometry. The vitamin B12 present in the yolk or white of century eggs was recovered completely in macromol. fractions, but not in free vitamin B12 fractions by Sephadex G-50 gel filtration. However, with respect to the vitamin B12 bound to protein in the century egg yolk, approx. 52% of the free vitamin B12 was formed during in vitro gastric digestion and no free vitamin B12 was detected in the egg white.
- 27Baik, H. W.; Russell, R. M. Vitamin B12 deficiency in the elderly. Annu. Rev. Nutr. 1999, 19, 357– 377, DOI: 10.1146/annurev.nutr.19.1.357Google Scholar27Vitamin B12 deficiency in the elderlyBaik, H. W.; Russell, R. M.Annual Review of Nutrition (1999), 19 (), 357-377CODEN: ARNTD8; ISSN:0199-9885. (Annual Reviews Inc.)A review with 153 refs. Vitamin B12 deficiency affects 10-15% people over the age of 60, and the lab. diagnosis is usually based on low blood serum vitamin B12 levels or elevated serum methylmalonic acid and homocysteine levels. Although elderly people with low vitamin B12 status frequently lack the classical signs and symptoms of vitamin B12 deficiency (megaloblastic anemia), precise evaluation and treatment in this population is important. Absorption of cryst. vitamin B12 does not decline with advancing age. Compared with the younger population, the absorption of protein-bound vitamin B12 is decreased in the elderly due to a high prevalence of atrophic gastritis in this age group. Atrophic gastritis results in a low acid-pepsin secretion by the gastric mucosa, which in turn decreases the release of free vitamin B12 from food proteins. Hypochlorhydria in atrophic gastritis results in bacterial overgrowth in the stomach and small intestine, and the bacteria may bind vitamin B12 for their own use. The ability to absorb cryst. vitamin B12 remains intact in older people with atrophic gastritis. The 1998 recommended daily allowance for vitamin B12 is 2.4 μg, but elderly people should try to obtain their vitamin B12 from supplements or fortified foods (e.g. fortified ready-to-eat breakfast cereals) to ensure adequate absorption from the gastrointestinal tract. Because the American food supply is now being fortified with folic acid, concern is increasing about neurol. exacerbation in individuals with marginal vitamin B12 status and high-dose folate intake.
- 28Malech, H. L.; Gallin, J. I. Neutrophils in human diseases. N. Engl. J. Med. 1987, 317, 687– 694, DOI: 10.1056/NEJM198709103171107Google Scholar28Current concepts: immunology. Neutrophils in human diseasesMalech H L; Gallin J IThe New England journal of medicine (1987), 317 (11), 687-94 ISSN:0028-4793.There is no expanded citation for this reference.
- 29Chapman, A. L.; Winterbourn, C. C.; Brennan, S. O.; Jordan, T. W.; Kettle, A. J. Characterization of non-covalent oligomers of proteins treated with hypochlorous acid. Biochem. J. 2003, 375, 33– 40, DOI: 10.1042/bj20030685Google Scholar29Characterization of non-covalent oligomers of proteins treated with hypochlorous acidChapman, Anna L. P.; Winterbourn, Christine C.; Brennan, Stephen O.; Jordan, T. William; Kettle, Anthony J.Biochemical Journal (2003), 375 (1), 33-40CODEN: BIJOAK; ISSN:0264-6021. (Portland Press Ltd.)Hypochlorous acid (HOCl) is a potent oxidant produced by myeloperoxidase that causes aggregation of many proteins. Treatment of apoHb and apomyoglobin with HOCl produced a regular series of oligomer bands when the proteins were sepd. by SDS-PAGE under reducing conditions. Aggregation was detectable at a HOCl/protein molar ratio of 0.5:1 and was maximal at ratios of 10:1-20:1. Dimers formed within 1 min of adding HOCl, and further aggregation occurred over the next 30 min. No convincing evidence for covalent crosslinking was obtained by amino acid anal., peptide anal. or electrospray ionization-MS of HOCl-modified apomyoglobin. The latter showed an increase in mass consistent with conversion of the two methionine residues into sulfoxides. A 5-fold excess of HOCl generated approx. three chloramines on the apomyoglobin. These underwent slow decay. Protein carbonyls were formed and were almost entirely located only on the polymer bands. Conversion of pos. into neg. charged groups on the protein by succinylation caused preformed aggregates to dissoc. Treatment of apomyoglobin with taurine chloramine generated methionine sulfoxides but few protein carbonyls, and did not result in aggregation. We conclude that aggregation was due to strong, non-covalent interactions between protein chains. We propose that formation of protein carbonyls and possibly chloramines, along with methionine oxidn., alters protein folding to expose hydrophobic areas on neighboring mols. that assoc. to form dimers and higher-mol.-mass aggregates. This process could lead to the formation of aggregated proteins at sites of myeloperoxidase activity and contribute to inflammatory tissue injury.
- 30Scheuring, E. M.; Sagi, I.; Chance, M. R. Sulur-containing cobalamins: X-ray absorption spectroscopic characterization. Biochemistry 1994, 33, 6310– 6315, DOI: 10.1021/bi00186a034Google Scholar30Sulfur-Containing Cobalamins: X-ray Absorption Spectroscopic CharacterizationScheuring, Eva M.; Sagi, Irit; Chance, Mark R.Biochemistry (1994), 33 (20), 6310-15CODEN: BICHAW; ISSN:0006-2960.Sulfur-contg. cobalamins are thought to have a special role in the intracellular conversion of cyanocobalamin to its coenzyme forms through a Co(I) intermediate. Glutathionylcobalamin is esp. interesting as a possible precursor of cobalamin coenzymes [Wagner et al. (1969) Ann. N.Y.Acad. Sci. 112, 580; Pezacka et al. (1990) Biochem. Biophys. Res. Commun. 169, 443]. Recent NMR data [Brown et al. (1993) Biochem. 32, 8421] strongly support the hypothesis that glutathione coordinates to the cobalt through the sulfur atom in glutathionylcobalamin. In this study three-sulfur contg. cobalamin derivs.(glutathionylcobalamin, sulfitocobalamin, and cysteinylcobalamin) have been characterized by X-ray absorption spectroscopy. The authors give evidence for the sulfur coordination in these compds. and present the corresponding structural information. The Co-Neq distances in the sulfur-contg. cobalamins are very close to one another (1.90 ± 0.01 Å). The Co-S and Co-Nax distances are also similar (Co-S: 2.28-2.35Å and Co-Nax: 2.13-2.16 6 Å) and in the expected range. The X-ray edge positions for the sulfur derivs. shift to lower energies with respect to cyanocobalamin. This indicates strong electron donation from the sulfur to the cobalt and suggests that the effective charge on the cobalt ion in sulfur cobalamins is largely reduced from +3.
- 31Pezacka, E.; Green, R.; Jacobsen, D. W. Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymes. Biochem. Biophys. Res. Commun. 1990, 169, 443– 450, DOI: 10.1016/0006-291X(90)90351-MGoogle Scholar31Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymesPezacka, Ewa; Green, Ralph; Jacobsen, Donald W.Biochemical and Biophysical Research Communications (1990), 169 (2), 443-50CODEN: BBRCA9; ISSN:0006-291X.To evaluate the possible role of glutathionylcobalamin (GS-Cbl) in the intracellular metab. of cobalamin, the following reactions were analyzed using exts. of rabbit spleen: (1) decyanation of cyanocobalamin; (2) utilization of GS-Cbl by cobalamin reductase; (3) participation of GS-Cbl in methionine biosynthesis; and (4) conversion of GS-Cbl to adensoylcobalamin. Decyanation of cyanocobalamin required reduced glutathione which appeared to form a complex with the cobalamin. This complex decompd. during the extn. steps to sulfitocobalamin which was identified by HPLC. Cobalamin reductase in spleen ext. was more active with GS-Cbl than with aquocobalamin or cyanocobalamin as substrates (specific activities: 10.4, 2.8, and 0.93 nmol/mg/min, resp.). Methionine synthase utilized GS-Cbl as cofactor more efficiently than aquocobalamin or cyanocobalamin based on initial rates of enzyme activity. This suggests that GS-Cbl is a more direct precursor of the coenzyme required for methionine synthase. Formation of adenosylcobalamin from GS-Cbl was 4-times greater than from aquocobalamin alone. Based on these results, it is proposed that GS-Cbl or a closely related thiol-cobalamin adduct is a proximal precursor in cobalamin coenzyme biosynthesis.
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- Huan Feng, Jianping Liu, Ali Qaitoon, Qingtao Meng, Yasmina Sultanbawa, Zhiqiang Zhang, Zhi Ping Xu, Run Zhang. Responsive small-molecule luminescence probes for sulfite/bisulfite detection in food samples. TrAC Trends in Analytical Chemistry 2021, 136 , 116199. https://doi.org/10.1016/j.trac.2021.116199
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Abstract
Figure 1
Figure 1. UV–visible absorption spectra of CN-B12 after treatment with these food additives. CN-B12 was dissolved in hypochlorous acid water (at an effective chlorine concentration of 30 ppm) (A), 0.01% (w/v) sodium metabisulfite (B), and 0.01% (w/v) solution sodium sulfite (C) solutions at a final concentration of 10 μmol/L. These solutions were left for 0 h (—), 1 h (− − −), 24 h (- - -), and 48 h (······) at room temperature (25 °C). A solution of CN-B12 treated without these food additives was used as control (—). At the indicated time points, the UV–visible absorption spectra of these solutions were measured using a UV–visible spectrophotometer. These are typical spectrophotometric data obtained from three independent experiments.
Figure 2
Figure 2. HPLC patterns of the B12 compounds treated with hypochlorous acid water. CN-B12 was dissolved in hypochlorous acid water (at an effective chlorine concentration of 10 ppm) at a final concentration of 10 μmol/L and left for 1 h at room temperature (25 °C) in the dark. The CN-B12 solution was loaded onto a Sep-Pak Vac (5 g) C18 cartridge to remove the hypochlorous acid. The fraction of the B12 compounds was dissolved in a small amount of water and subsequently used as a sample for HPLC analysis. An aliquot (30 μL) of the sample was placed on a reversed-phase HPLC column. The B12 compounds were eluted for 20 min with a linear gradient of 20–90% (v/v) methanol solution containing 1% (v/v) acetic acid, followed by elution with 90% (v/v) methanol solution containing 1% (v/v) acetic acid for 10 min, and were monitored by measuring the absorbance at 361 nm. The HPLC patterns of the B12 compounds are typical data obtained from three independent experiments.
Figure 3
Figure 3. 1H NMR spectrum of authentic CN-B12.
Figure 4
Figure 4. 1H NMR spectra of B12 compounds formed during treatment with hypochlorous acid water. (A), Compound P-2 (with a retention time of 10.9 min); (B), compound P-3 (with a retention time of 12.3 min); and (C) compound P-6 (with a retention time of 17.1 min).
Figure 5
Figure 5. HPLC patterns of the B12 compounds treated with 0.01% (w/v) sodium metabisulfite. CN-B12 was dissolved in 0.01% (w/v) sodium metabisulfite solution at a final concentration of 10 μmol/L and left for 48 h at room temperature (25 °C) in the dark. (A) Treated CN-B12 solution (50 μL) or (B) authentic sulfitocobalamin (20 μL of 130 mg/L) was loaded onto a reversed-phase HPLC column. The B12 compounds were isocratically eluted and monitored by measuring the absorbance at 361 nm. Data are typical HPLC patterns of the B12 compounds treated with sodium metabisulfite or authentic sulfitocobalamin obtained from three independent experiments.
Figure 6
Figure 6. Effects of the B12 compounds treated with hypochlorous acid water on B12-dependent E. coli 215. (A) Authentic B12 (100 pg) and (B) hypochlorous acid-treated B12 compounds after purification using a Sep-Pak Vac (5 g) C18 cartridge.
Figure 7
Figure 7. Effects of treatment with hypochlorous acid water, sodium metabisulfite, and sodium sulfite on the B12 content of red shrimp meat. The edible portion of Argentine red shrimps was collected and homogenized using a mortar and pestle. The shrimp meat homogenate (10 g) was treated with 1.0 mL of distilled water as a control (1), hypochlorous acid water (at an effective chlorine concentration of 30 ppm) (2), 0.1% (w/v) sodium metabisulfite solution (3), and 0.1% (w/v) sodium sulfite solution (4) and subsequently mixed. Three sets of putties (3 × 3 × 1 cm3) from each sample were formed and then allowed to stand at 4 °C for 48 h in the dark. The B12 was extracted from each stored sample, and its amount was determined using L. delbrueckii ATCC 7830 bioassay. B12 content was assayed in triplicate. Data are represented as means ± SEM (n = 3).
Figure 8
Figure 8. Effects of various concentrations of hypochlorous acid water on the B12 content of ground beef meat. Ground beef meat (10 g) was treated with 1.0 mL of distilled water as a control (1) and treated with 1.0 mL of hypochlorous acid water at effective chlorine concentrations of 30 ppm (2), 60 ppm (3), and 80 ppm (4) and subsequently mixed. Three sets of putties (3 × 3 × 1 cm3) from each sample were formed and then allowed to stand at 4 °C for 48 h in the dark. B12 was extracted from each stored sample, and its amount was determined using L. delbrueckii ATCC 7830 bioassay. B12 content was assayed in triplicate. Data are represented as means ± SEM (n = 3).
References
This article references 31 other publications.
- 1Watanabe, F.; Bito, T. Corrinoids in Food and Biological Samples, In Frontiers in Natural Product Chemistry, Atta-ur-Rahman, F. R. S., Eds.; Bentham Science, 2016; Vol. 2, pp 229– 244.There is no corresponding record for this reference.
- 2Watanabe, F.; Bito, T. Vitamin B12 sources and microbial interaction. Exp. Biol. Med. 2018, 243, 148– 158, DOI: 10.1177/15353702177466122Vitamin B12 sources and microbial interactionWatanabe, Fumio; Bito, TomohiroExperimental Biology and Medicine (London, United Kingdom) (2018), 243 (2), 148-158CODEN: EBMMBE; ISSN:1535-3699. (Sage Publications Ltd.)Vitamin B12 is synthesized only by certain bacteria and archaeon, but not by plants. The synthesized vitamin B12 is transferred and accumulates in animal tissues, which can occur in certain plant and mushroom species through microbial interaction. In particular, the meat and milk of herbivorous ruminant animals (e.g. cattle and sheep) are good sources of vitamin B12 for humans. Ruminants acquire vitamin B12, which is considered an essential nutrient, through a symbiotic relationship with the bacteria present in their stomachs. In aquatic environments, most phytoplankton acquire vitamin B12 through a symbiotic relationship with bacteria, and they become food for larval fish and bivalves. Edible plants and mushrooms rarely contain a considerable amt. of vitamin B12, mainly due to concomitant bacteria in soil and/or their aerial surfaces. Thus, humans acquire vitamin B12 formed by microbial interaction via mainly ruminants and fish (or shellfish) as food sources. In this review, up-to-date information on vitamin B12 sources and bioavailability are also discussed. To prevent vitamin B12 (B12) deficiency in high-risk populations such as vegetarians and elderly subjects, it is necessary to identify foods that contain high levels of B12. B12 is synthesized by only certain bacteria and archaeon, but not by plants or animals. The synthesized B12 is transferred and accumulated in animal tissues, even in certain plant tissues via microbial interaction. Meats and milks of herbivorous ruminant animals are good sources of B12 for humans. Ruminants acquire the essential B12 through a symbiotic relationship with bacteria inside the body. Thus, we also depend on B12-producing bacteria located in ruminant stomachs. While edible plants and mushrooms rarely contain a considerable amt. of B12, mainly due to concomitant bacteria in soil and/or their aerial surfaces. In this mini-review, we described up-to-date information on B12 sources and bioavailability with ref. to the interaction of microbes as B12-producers.
- 3Watanabe, F. Vitamin B12 sources and bioavailability. Exp. Biol. Med. 2007, 232, 1266– 1274, DOI: 10.3181/0703-MR-673Vitamin B12 sources and bioavailabilityWatanabe, FumioExperimental Biology and Medicine (Maywood, NJ, United States) (2007), 232 (10), 1266-1274CODEN: EBMMBE; ISSN:1535-3702. (Society for Experimental Biology and Medicine)A review. The usual dietary sources of vitamin B12 are animal foods, meat, milk, egg, fish, and shellfish. As the intrinsic factor-mediated intestinal absorption system is estd. to be satd. at about 1.5-2.0 μg per meal under physiol. conditions, vitamin B12 bioavailability significantly decreases with increasing intake of vitamin B12 per meal. The bioavailability of vitamin B12 in healthy humans from fish meat, sheep meat, and chicken meat averaged 42%, 56%-89%, and 61%-66%, resp. Vitamin B12 in eggs seems to be poorly absorbed (<9%) relative to other animal food products. In the Dietary Ref. Intakes in the United States and Japan, it is assumed that 50% of dietary vitamin B12 is absorbed by healthy adults with normal gastrointestinal function. Some plant foods, dried green and purple lavers (nori) contain substantial amts. of vitamin B12, although other edible algae contained none or only traces of vitamin B12. Most of the edible blue-green algae (cyanobacteria) used for human supplements predominately contain pseudovitamin B12, which is inactive in humans. The edible cyanobacteria are not suitable for use as vitamin B12 sources, esp. in vegans. Fortified breakfast cereals are a particularly valuable source of vitamin B12 for vegans and elderly people. Prodn. of some vitamin B12-enriched vegetables is also being devised.
- 4Bito, T.; Watanabe, F.; Tanioka, Y. Characterization of vitamin B12 compounds from marine foods. Fish. Sci. 2018, 84, 747– 755, DOI: 10.1007/s12562-018-1222-54Characterization of vitamin B12 compounds from marine foodsBito, Tomohiro; Tanioka, Yuri; Watanabe, FumioFisheries Science (Tokyo, Japan) (2018), 84 (5), 747-755CODEN: FSCIEH; ISSN:0919-9268. (Springer Japan)A review. Vitamin B12 is synthesized by only certain bacteria and archaea but not by animals or plants. In marine environments, bacterial vitamin B12 is transferred and concd. into fish and shellfish bodies by plankton in the marine food chain. Moreover, marine macrophytic red algae, Porphyra spp. specifically contain substantial amts. of vitamin B12, due to microbial interaction. Although some meats or viscera of edible fish and shellfish are excellent sources of biol. active vitamin B12, an inactive corrinoid, pseudovitamin B12, was found in some edible shellfish using liq. chromatog./electrospray ionization-tandem mass spectrometry. To prevent elderly people from developing vitamin B12 deficiency due to food protein-bound vitamin B12 malabsorption, we present a survey of marine foods contg. free vitamin B12. The results of our study suggest that bonito and clam exts. (or soup stocks), which contain considerable amts. of free vitamin B12 are useful not only as seasonings and flavorings but also as excellent sources of free vitamin B12.
- 5Watanabe, F.; Yabuta, Y.; Tanioka, Y.; Bito, T. Biologically active vitamin B12 compounds in foods for preventing deficiency among vegetarians and elderly subjects. J. Agric. Food Chem. 2013, 61, 6769– 6775, DOI: 10.1021/jf401545z5Biologically Active Vitamin B12 Compounds in Foods for Preventing Deficiency among Vegetarians and Elderly SubjectsWatanabe, Fumio; Yabuta, Yukinori; Tanioka, Yuri; Bito, TomohiroJournal of Agricultural and Food Chemistry (2013), 61 (28), 6769-6775CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)A review. The usual dietary sources of vitamin B12 are animal-source based foods, including meat, milk, eggs, fish, and shellfish, although a few plant-based foods such as certain types of dried lavers (nori) and mushrooms contain substantial and considerable amts. of vitamin B12, resp. Unexpectedly, detailed characterization of vitamin B12 compds. in foods reveals the presence of various corrinoids that are inactive in humans. The majority of edible blue-green algae (cyanobacteria) and certain edible shellfish predominately contain an inactive corrinoid known as pseudovitamin B12. Various factors affect the bioactivity of vitamin B12 in foods. For example, vitamin B12 is partially degraded and loses its biol. activity during cooking and storage of foods. The intrinsic factor-mediated gastrointestinal absorption system in humans has evolved to selectively absorb active vitamin B12 from naturally occurring vitamin B12 compds., including its degrdn. products and inactive corrinoids that are present in daily meal foods. The objective of this review is to present up-to-date information on various factors that can affect the bioactivity of vitamin B12 in foods. To prevent vitamin B12 deficiency in high-risk populations such as vegetarians and elderly subjects, it is necessary to identify plant-source foods that contain high levels of bioactive vitamin B12 and, in conjunction, to prep. the use of cryst. vitamin B12-fortified foods.
- 6Watanabe, F.; Katsura, H.; Takenaka, S.; Fujita, T.; Abe, K.; Tamura, Y.; Nakatsuka, T.; Nakano, Y. Pseudovitamin B12 is the predominant cobamide of an algal health food, Spirulina Tablets. J. Agric. Food Chem. 1999, 47, 4736– 4741, DOI: 10.1021/jf990541b6Pseudovitamin B12 Is the Predominant Cobamide of an Algal Health Food, Spirulina TabletsWatanabe, Fumio; Katsura, Hiromi; Takenaka, Shigeo; Fujita, Tomoyuki; Abe, Katsuo; Tamura, Yoshiyuki; Nakatsuka, Toshiyuki; Nakano, YoshihisaJournal of Agricultural and Food Chemistry (1999), 47 (11), 4736-4741CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)The vitamin B12 concn. of an algal health food, Spirulina (Spirulina sp.) tablets, was detd. by both Lactobacillus leichmannii ATCC 7830 microbiol. and intrinsic factor chemiluminescence methods. The values detd. with the microbiol. method were ∼6-9-fold greater in the Spirulina tablets than the values detd. with the chemiluminescence method. Although most of the vitamin B12 detd. with the microbiol. method was derived from various vitamin B12 substitutive compds. and/or inactive vitamin B12 analogs, the spirulina contained a small amt. of vitamin B12 active in the binding of the intrinsic factor. Two intrinsic factor active vitamin B12 analogs (major and minor) were purified from the spirulina tablets and partially characterized. The major (83%) and minor (17%) analogs were identified as pseudovitamin B12 and vitamin B12, resp., as judged from data of TLC, reversed-phase HPLC, 1H NMR spectroscopy, UV-visible spectroscopy, and biol. activity using L. leichmannii as a test organism and the binding of vitamin B12 to the intrinsic factor.
- 7Miyamoto, E.; Tanioka, Y.; Nakao, T.; Barla, F.; Inui, H.; Fujita, T.; Watanabe, F.; Nakano, Y. Purification and characterization of a corrinoid-compound in an edible cyanobacterium Aphanizomenon flos-aquae as a nutritional supplementary food. J. Agric. Food Chem. 2006, 54, 9604– 9607, DOI: 10.1021/jf062300r7Purification and characterization of a corrinoid compound in an edible Cyanobacterium Aphanizomenon flos-aquae as a nutritional supplementary foodMiyamoto, Emi; Tanioka, Yuri; Nakao, Tomoyuki; Barla, Florin; Inui, Hiroshi; Fujita, Tomoyuki; Watanabe, Fumio; Nakano, YoshihisaJournal of Agricultural and Food Chemistry (2006), 54 (25), 9604-9607CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)The vitamin B12 concn. of the dried cells of Aphanizomenon flos-aquae was detd. by both microbiol. method with Lactobacillus delbrueckii ATCC7830 and chemiluminescence method with intrinsic factor. The Aphanizomenon cells contained 616.3 ± 30.3 μg (n = 4) of vitamin B12 per 100 g of the dried cells by the microbiol. method. The values detd. with the chemiluminescence method, however, were only about 5.3% of the values detd. by the microbiol. method. A corrinoid compd. was purified from the dried cells and characterized. The purified corrinoid compd. was identified as pseudovitamin B12 (an inactive corrinoid compd. for humans) by silica gel 60 TLC, C18 reversed-phase HPLC, UV-visible spectroscopy, and 1H NMR spectroscopy. The results suggest that the Aphanizomenon cells are not suitable for use as a vitamin B12 source, esp. in vegans.
- 8Teng, F.; Tanioka, Y.; Hamaguchi, N.; Bito, T.; Takenaka, S.; Yabuta, Y.; Watanabe, F. Determination and characterization of vitamin B12 compounds in edible sea snails, ivory shell Babylonia japonica and turban shell Turdo Batillus cornutus. Fish. Sci. 2015, 81, 1105– 1111, DOI: 10.1007/s12562-015-0920-58Determination and characterization of vitamin B12 compounds in edible sea snails, ivory shell Babylonia japonica and turban shell Turdo Batillus cornutusTeng, Fei; Tanioka, Yuri; Hamaguchi, Natsumi; Bito, Tomohiro; Takenaka, Shigeo; Yabuta, Yukinori; Watanabe, FumioFisheries Science (Tokyo, Japan) (2015), 81 (6), 1105-1111CODEN: FSCIEH; ISSN:0919-9268. (Springer Japan)In this study, we characterized and quantified vitamin B12 compds. in popular edible snails Babylonia japonica and Turdo Batillus cornutus using a microbiol. assay based on Lactobacillus delbrueckii subsp. lactis ATCC 7830. The meat and viscera of B. japonica contained 27.2 ± 9.1 and 92.8 ± 25.8 μg of vitamin B12 per 100 g, resp. However, the meat and viscera of T. cornutus contained extremely low amts. of vitamin B12 (3.0 ± 1.5 and 15.1 ± 8.3 μg of vitamin B12 per 100 g, resp.). We identified the vitamin B12 compds. from the edible portions (meat and viscera) of B. japonica and T. cornutus using liq. chromatog.-electrospray ionization/tandem mass spectrometry. We found that B. japonica contained substantial amts. of true vitamin B12, while pseudovitamin B12 was the predominant corrinoid in T. cornutus. These results indicate that the meat and viscera of B. japonica are excellent sources of vitamin B12 for humans.
- 9Bito, T.; Teng, F.; Ohishi, N.; Takenaka, S.; Miyamoto, E.; Sakuno, E.; Terashima, K.; Yabuta, Y.; Watanabe, F. Characterization of vitamin B12 compounds in the fruiting bodies of shiitake mushroom (Lentinura edodes) and bed logs after fruiting of the mushroom. Mycoscience 2014, 55, 462– 468, DOI: 10.1016/j.myc.2014.01.0089Characterization of vitamin B12 compounds in the fruiting bodies of shiitake mushroom (Lentinula edodes) and bed logs after fruiting of the mushroomBito, Tomohiro; Teng, Fei; Ohishi, Noriharu; Takenaka, Shigeo; Miyamoto, Emi; Sakuno, Emi; Terashima, Kazuhisa; Yabuta, Yukinori; Watanabe, FumioMycoscience (2014), 55 (6), 462-468CODEN: MNCEED; ISSN:1340-3540. (Elsevier Japan K. K.)This study detd. the vitamin B12 content in com. available dried fruiting bodies of shiitake mushroom, Lentinula edodes. The vitamin B12 contents in dried donko-type fruiting bodies with closed caps (5.61 ± 3.90 μg/100 g dry wt.), did not significantly differ from those of dried koushin-type fruiting bodies with open caps (4.23 ± 2.42 μg/100 g dry wt.). The bed logs after fruiting of the mushroom also contained the vitamin B12 levels similar to that in the dried shiitake fruiting bodies. To det. whether the dried shiitake fruiting bodies and their bed logs contained vitamin B12 or other corrinoid compds. that are inactive in humans, we purified corrinoid compds. using an immunoaffinity column and identified vitamin B12 using vitamin B12-dependent Escherichia coli 215 bioautograms and liq. chromatog.-electrospray ionization tandem mass spectrometry (LC/ESI-MS/MS) chromatograms. Dried shiitake fruiting bodies rarely contained an unnatural corrinoid vitamin B12[c-lactone] that is inactive in humans. Given that shiitake mushroom lacks the ability to synthesize vitamin B12de novo, the vitamin B12 found in dried shiitake fruiting bodies must have been derived from the bed logs.
- 10Teng, F.; Bito, T.; Takenaka, S.; Yabuta, Y.; Watanabe, F. Vitamin B12[c-lactone], a biologically inactive corrinoid compound, occurs in cultured and dried lion’s mane mushroom (Hericium erinaceus) fruiting bodies. J. Agric. Food Chem. 2014, 62, 1726– 1732, DOI: 10.1021/jf404463v10Vitamin B12[c-lactone], a Biologically Inactive Corrinoid Compound, Occurs in Cultured and Dried Lion's Mane Mushroom (Hericium erinaceus) Fruiting BodiesTeng, Fei; Bito, Tomohiro; Takenaka, Shigeo; Yabuta, Yukinori; Watanabe, FumioJournal of Agricultural and Food Chemistry (2014), 62 (7), 1726-1732CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)This study detd. the vitamin B12 content of the edible medicinal mushroom Hericium erinaceus, lion's mane mushroom fruiting body, using a microbiol. assay based on Lactobacillus delbrueckii ATCC 7830. Trace levels (0.04-0.36 μg/100 g dry wt.) of vitamin B12 were found in most of the dried mushroom samples, and two samples contained slightly higher levels (0.56 and 1.04 μg/100 g dry wt., resp.) of vitamin B12. We purified the corrinoid compds. from the exts. of dried lion's mane mushroom fruiting bodies using an immunoaffinity column and identified them as vitamin B12 or vitamin B12[c-lactone] (or both) based on LC/ESI-MS/MS chromatograms. This is the first report on an unnatural corrinoid, vitamin B12[c-lactone], occurring in foods. Vitamin B12[c-lactone] was simple to produce during incubation of authentic vitamin B12 and chloramine-T, an antimicrobial agent, at varying pH values (3.0-7.0) and was completely inactive in the vitamin B12-dependent bacteria that are generally used in vitamin B12 bioassays.
- 11Hakim, H.; Alam, M. S.; Sangsriratanakul, N.; Nakajima, K.; Kitazawa, M.; Ota, M.; Toyofuku, C.; Yamada, M.; Thammakarn, C.; Shoham, D.; Takehara, K. Inactivation of bacteria on surfaces by sprayed slightly acidic hypochlorous acid water: in vitro experiments. J. Vet. Med. Sci. 2016, 78, 1123– 1128, DOI: 10.1292/jvms.16-007511Inactivation of bacteria on surfaces by sprayed slightly acidic hypochlorous acid water: in vitro experimentsHakim, Hakimullah; Alam, Md. Shahin; Sangsriratanakul, Natthanan; Nakajima, Katsuhiro; Kitazawa, Minori; Ota, Mari; Toyofuku, Chiharu; Yamada, Masashi; Thammakarn, Chanathip; Shoham, Dany; Takehara, KazuakiJournal of Veterinary Medical Science (2016), 78 (7), 1123-1128CODEN: JVMSEQ; ISSN:0916-7250. (Japanese Society of Veterinary Science)The capacity of slightly acidic hypochlorous acid water (SAHW), in both liq. and spray form, to inactivate bacteria was evaluated as a potential candidate for biosecurity enhancement in poultry prodn. SAHW (contg. 50 or 100 ppm chlorine, pH 6) was able to inactivate Escherichia coli and Salmonella Infantis in liq. to below detectable levels (≤2.6 log10 CFU/mL) within 5 s of exposure. In addn., SAHW antibacterial capacity was evaluated by spraying it using a nebulizer into a box contg. these bacteria, which were present on the surfaces of glass plates and rayon sheets. SAHW was able to inactivate both bacterial species on the glass plates (dry condition) and rayon sheets within 5 min spraying and 5 min contact times, with the exception of 50 ppm SAHW on the rayon sheets. Furthermore, a corrosivity test detd. that SAHW does not corrode metallic objects, even at the longest exposure times (83 days). Our findings demonstrate that SAHW is a good candidate for biosecurity enhancement in the poultry industry. Spraying it on the surfaces of objects, eggshells, egg incubators and transport cages could reduce the chances of contamination and disease transmission. These results augment previous findings demonstrating the competence of SAHW as an anti-viral disinfectant.
- 12Veasey, S.; Muriana, P. M. Evaluation of electrolytically-generated hypochlorous acid (‘Electrolyzed water’) for sanitation of meat and meat-contact surfaces. Foods 2016, 5, 42, DOI: 10.3390/foods502004212Evaluation of electrolytically-generated hypochlorous acid ('electrolyzed water') for sanitation of meat and meat-contact surfacesVeasey, Shawnna; Muriana, Peter M.Foods (2016), 5 (2), 42/1-42/15CODEN: FOODBV; ISSN:2304-8158. (MDPI AG)'Electrolyzed water' generators are readily available in the food industry as a renewable source of hypochlorous acid that eliminates the need for workers to handle hazardous hypochlorite concs. We applied electrolyzed water (EW) directly to multi-strain cocktails of Listeria monocytogenes, E. coli O157:H7, and Salmonella sp. at 250 ppm free available chlorine (FAC) and achieved greater than 6-log redns. in 2 min. Lower EW values were examd. as antimicrobial interventions for fresh meat (beef carcasses), processed meats (frankfurters), and food contact surfaces (slicing blades). Little or no redn. relative to controls was obsd. when generic E. coli-inoculated beef carcasses or L. monocytogenes-inoculated frankfurters were showered with EW. Spray application of EW (25 and 250-ppm FAC) onto L. monocytogenes-inoculated slicing blades showed that greater redns. were obtained with 'clean' (3.6 and 5.7-log redn.) vs. 'dirty' (0.6 and 3.3-log redn.) slicing blades, resp. Trials with L. monocytogenes-inoculated protein-EW solns. demonstrated that protein content as low as 0.1% is capable of eliminating FAC, reducing antimicrobial activity against L. monocytogenes. EW appears better positioned as a surface sanitizer with minimal org. material that can otherwise act as an effective reducing agent to the oxidizing soln. rendering it ineffective.
- 13Quan, Y.; Kim, H.-Y.; Shin, I.-S. Bactericidal activity of strong acidic hypochlorous water against Escherichia coli O157:H7 and Listeria monocytogenes in biofilms attached to stainless steel. Food Sci. Biotechnol. 2017, 26, 841– 846, DOI: 10.1007/s10068-017-0086-213Bactericidal activity of strong acidic hypochlorous water against Escherichia coli O157:H7 and Listeria monocytogenes in biofilms attached to stainless steelQuan, Yaru; Kim, Hee-Yeon; Shin, Il-ShikFood Science and Biotechnology (2017), 26 (3), 841-846CODEN: FSBOBR; ISSN:1226-7708. (Korean Society of Food Science and Technology)This study aims to investigate the bactericidal activity of strong acidic hypochlorous water (SAHW) against Escherichia coli O157:H7 and L. monocytogenes in bacterial biofilms. The bactericidal activity of SAHW against both bacteria in colony biofilm increased with the elevation of the available chlorine concn. (ACC) and extension of the treatment time. The survived cell counts of E. coli O157:H7 and L. monocytogenes in the biofilms were significantly (p < 0.05) decreased compare to tap water at more than 30 mg/L of ACC in SAHW and 15 s of treatment time. E. coli O157:H7 and L. monocytogenes in the biofilms reduced to less than the detection limit by treatment of 50 mg/L of ACC in SAHW for 300 and 600 s, resp. SAHW may be a potential disinfecting agent for removing bacterial biofilms from food processing equipment and other facilities.
- 14Pattison, D. I.; Davies, M. J. Absolute rate constants for the reaction of hypochlours acid with protein side chains and peptide bonds. Chem. Res. Toxicol. 2001, 14, 1453– 1464, DOI: 10.1021/tx015545114Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bondsPattison, David I.; Davies, Michael J.Chemical Research in Toxicology (2001), 14 (10), 1453-1464CODEN: CRTOEC; ISSN:0893-228X. (American Chemical Society)Hypochlorous acid (HOCl) is a potent oxidant, which is produced in vivo by activated phagocytes. This compd. is an important antibacterial agent, but excessive or misplaced prodn. has been implicated in a no. of human diseases, including atherosclerosis, arthritis, and some cancers. Proteins are major targets for this oxidant, and such reaction results in side-chain modification, backbone fragmentation, and crosslinking. Despite a wealth of qual. data for such reactions, little abs. kinetic data is available to rationalize the in vitro and in vivo data. In this study, abs. second-order rate consts. for the reactions of HOCl with protein side chains, model compds., and backbone amide (peptide) bonds have been detd. at physiol. pH values. The reactivity of HOCl with potential reactive sites in proteins is summarized by the series: Met (3.8 × 107 M-1 s-1) > Cys (3.0 × 107 M-1 s-1) » cystine (1.6 × 105 M-1 s-1) ≈ His (1.0 × 105 M-1 s-1) ≈ α-amino (1.0 × 105 M-1 s-1) > Trp (1.1 × 104 M-1 s-1) > Lys (5.0 × 103 M-1 s-1) » Tyr (44 M-1 s-1) ≈ Arg (26 M-1 s-1) > backbone amides (10-10-3 M-1 s-1) > Gln (0.03 M-1 s-1) ≈ Asn (0.03 M-1 s-1). The rate consts. for reaction of HOCl with backbone amides (peptide bonds) vary by 4 orders of magnitude with uncharged peptide bonds reacting more readily with HOCl than those in a charged environment. These kinetic parameters have been used in computer modeling of the reactions of HOCl with human serum albumin, apolipoprotein-A1 and free amino acids in plasma at different molar excesses. These models are useful tools for predicting, and reconciling, exptl. data obtained in HOCl-induced oxidns. and allow estns. to be made as to the flux of HOCl to which proteins are exposed in vivo.
- 15Kerkaert, B.; Mestdagh, F.; Cucu, T.; Aedo, P. R.; Ling, S. Y.; De Meulenaer, B. Hypochlorous and peracetic acid induced oxidation of dairy proteins. J. Agric. Food Chem. 2011, 59, 907– 914, DOI: 10.1021/jf103780715Hypochlorous and Peracetic Acid Induced Oxidation of Dairy ProteinsKerkaert, Barbara; Mestdagh, Frederic; Cucu, Tatiana; Aedo, Philip Roger; Ling, Shen Yan; De Meulenaer, BrunoJournal of Agricultural and Food Chemistry (2011), 59 (3), 907-914CODEN: JAFCAU; ISSN:0021-8561. (American Chemical Society)Hypochlorous and peracetic acids, both known disinfectants in the food industry, were compared for their oxidative capacity toward dairy proteins. Whey proteins and caseins were oxidized under well controlled conditions at pH 8 as a function of the sanitizing concn. Different markers for protein oxidn. were monitored. The results established that the protein carbonyl content was a rather unspecific marker for protein oxidn., which did not allow one to differentiate the oxidant used esp. at the lower concns. Cysteine, tryptophan, and methionine were proven to be the most vulnerable amino acids for degrdn. upon hypochlorous and peracetic acid treatment, while tyrosine was only prone to degrdn. in the presence of hypochlorous acid. Hypochlorous acid induced oxidn. gave rise to protein aggregation, while during peracetic acid induced oxidn., no high mol. wt. aggregates were obsd. Protein aggregation upon hypochlorous acid oxidn. could primarily be linked to tryptophan and tyrosine degrdn.
- 16Vandekinderen, I.; Van Camp, J.; Devlieghere, F.; Veramme, K.; Bernaert, N.; Denon, Q.; Ragaert, P.; De Meulenaer, B. Effect of decontamination on the microbial load, the sensory quality and the nutrient retention of ready-to-eat white cabbage. Eur. Food Res. Technol. 2009, 229, 443– 455, DOI: 10.1007/s00217-009-1069-116Effect of decontamination on the microbial load, the sensory quality and the nutrient retention of ready-to-eat white cabbageVandekinderen, Isabelle; Camp, John; Devlieghere, Frank; Veramme, Kim; Bernaert, Nathalie; Denon, Quenten; Ragaert, Peter; Meulenaer, BrunoEuropean Food Research and Technology (2009), 229 (3), 443-455CODEN: EFRTFO; ISSN:1438-2377. (Springer GmbH)The effect of different decontamination treatments such as washing with sodium hypochlorite (20 and 200 mg/L), peroxyacetic acid (80 and 250 mg/L), neutral electrolyzed oxidizing water (4.9 and 31.7 mg/L free chlorine) and contact with 1.55 mg/L chlorine dioxide gas on the microbial and sensory quality, and the nutrient content of fresh-cut white cabbage was studied. Only rinsing with 200 mg/L sodium hypochlorite, peroxyacetic acid or contact with gaseous chlorine dioxide resulted in significantly higher redns. of the total plate count (1.5-2.5 log cfu/g) than the ones achieved by washing with tap water (0.5 log cfu/g). However, those treatments giving the best results from a microbial point of view induced significant changes in the sensory quality. Regarding the effects on nutrient content, the mech. effects caused by water washing already reduced the vitamin C content by 16-29%. Contrary to washing with neutral electrolyzed oxidizing water and contact with chlorine dioxide gas, a supplementary decrease of the vitamin C content ranging between 9 and 28% was obsd., when peroxyacetic acid or 200 mg/L sodium hypochlorite were used. After the use of peroxyacetic acid or gaseous chlorine dioxide, the phenol content also showed a decreasing trend, although not statistically significant. Apart from the effect of washing with water, the lipophilic nutrients were well retained after a decontamination step except for the α-tocopherol content, when peroxyacetic acid was used (-43 to 56%), and for the all-trans-β-carotene content (-8%) of cabbage in contact with gaseous chlorine dioxide. Because of its potential to reduce the initial microbial load without neg. effects on the sensory quality, in combination with its limited effects on nutrient content, a treatment with 80 mg/L peroxyacetic acid is preferable to decontaminate fresh-cut white cabbage.
- 17Ahmadi, F.; Lee, Y. H.; Lee, W. H.; Oh, Y. K.; Park, K. K.; Kwak, W. S. Preservation of fruit and vegetable discards with sodium metabisulfite. J. Envrion. Manage. 2018, 224, 113– 121, DOI: 10.1016/j.jenvman.2018.07.044There is no corresponding record for this reference.
- 18Luo, X.-Y.; Tu, Y.-G.; Zhao, Y.; Li, J.-K.; Wang, J.-J. Effects of sulfhydryl compounds, carbohydrates, organic acids, and sodium sulfite on the formation of lysinoalamine in preserved egg. J. Food Sci. 2014, 79, 1621– 1629, DOI: 10.1111/1750-3841.1254318Effects of Sulfhydryl Compounds, Carbohydrates, Organic Acids, and Sodium Sulfite on the Formation of Lysinoalanine in Preserved EggLuo, Xu-ying; Tu, Yong-gang; Zhao, Yan; Li, Jian-ke; Wang, Jun-jieJournal of Food Science (2014), 79 (8), T1621-T1628CODEN: JFDSAZ; ISSN:0022-1147. (Wiley-Blackwell)To identify inhibitors for lysinoalanine formation in preserved egg, sulfhydryl compds. (glutathione, L-cysteine), carbohydrates (sucrose, D-glucose, maltose), org. acids (L-ascorbic acid, citric acid, DL-malic acid, lactic acid), and sodium sulfite were individually added at different concns. to a pickling soln. to prep. preserved eggs. Lysinoalanine formation as an index of these 10 substances was detd. Results indicate that glutathione, D-glucose, maltose, L-ascorbic acid, citric acid, lactic acid, and sodium sulfite all effectively diminished lysinoalanine formation in preserved egg albumen and yolk. When 40 and 80 mmol/L of sodium sulfite, citric acid, L-ascorbic acid, and D-glucose were individually added into the pickling soln., the inhibition rates of lysinoalanine in the produced preserved egg albumen and yolk were higher. However, the attempt of minimizing lysinoalanine formation was combined with the premise of ensuring preserved eggs quality. Moreover, the addn. of 40 and 80 mmol/L of sodium sulfite, 40 and 80 mmol/L of D-glucose, 40 mmol/L of citric acid, and 40 mmol/L of L-ascorbic acid was optimal to produce preserved eggs. The corresponding inhibition rates of lysinoalanine in the albumen were approx. 76.3% to 76.5%, 67.6% to 67.8%, 74.6%, and 74.6%, and the corresponding inhibition rates of lysinoalanine in the yolk were about 68.7% to 69.7%, 50.6% to 51.8%, 70.4%, and 57.8%. It was concluded that sodium sulfite, D-glucose, L-ascorbic, and citric acid at suitable concns. can be used to control the formation of lysinoalanine during preserved egg processing. Achieved results may be helpful to select several food ingredients or additives effective in inhibiting the toxic component lysinoalanine formation during preserved egg processing. Furthermore, it is geared toward building a lysinoalanine control system, and providing a theor. ref. for the processing of preserved egg.
- 19Suarez-Moreira, E.; Hannibal, L.; Smith, C. A.; Chavez, R. A.; Jacobsen, D. W.; Brasch, N. E. A simple, convenient method to synthesize cobalamins: synthesis of homocysteinylcobalamin, N-acetylcysteinylcobalamin, 2-N-acetylamino-2-carbomethoxyethanethiolatocobalamin, sulfitocobalamin and nitorocobalamin. Dalton Trans. 2006, 28, 5269– 5277, DOI: 10.1039/b610158eThere is no corresponding record for this reference.
- 20Tanioka, Y.; Yabuta, Y.; Miyamoto, E.; Inui, H.; Watanabe, F. Analysis of vitamin B12 in food by silica gel 60 TLC and bioautography with vitamin B12-dependent Escherichia coli 215. J. Liq. Chromatogr. Relat. Technol. 2008, 31, 1977– 1985, DOI: 10.1080/1082607080219745320Analysis of Vitamin B12 in Food by Silica Gel 60 TLC and Bioautography with Vitamin B12-Dependent Escherichia coli 215Tanioka, Yuri; Yabuta, Yukinori; Miyamoto, Emi; Inui, Hiroshi; Watanabe, FumioJournal of Liquid Chromatography & Related Technologies (2008), 31 (13), 1977-1985CODEN: JLCTFC; ISSN:1082-6076. (Taylor & Francis, Inc.)To evaluate whether certain foods contain vitamin B12 or inactive corrinoids, a simple technique, bioautog. with vitamin B12-dependent Escherichia coli mutant after sepn. of the sample by silica gel 60 thin-layer chromatog., is available. By using the method, vitamin B12-compds. found in some edible cyanobacteria are readily identified. This bioautog. has great advantages (simplicity, speed, and inexpensiveness) for the anal. of vitamin B12-compds. in food.
- 21Watanabe, F.; Bito, T. Determination of cobalamin and related compounds in foods. J. AOAC Int. 2018, 101, 1308– 1313, DOI: 10.5740/jaoacint.18-004521Determination of cobalamin and related compounds in foodsWatanabe, Fumio; Bito, TomohiroJournal of AOAC International (2018), 101 (5), 1308-1313CODEN: JAINEE; ISSN:1060-3271. (AOAC International)Cobalamin, also known as the red-colored vitamin B12, is found in animal-based foods such as meat, milk, and fish. Various cobalamin compds. are extd. from foods and converted into cyanocobalamin, which is most stable, to be analyzed by various methods. Traditionally, the cobalamin content of foods is detd. by microbiol. assay with Lactobacillus delbrueckii subsp. lactis American Type Culture Collection 7830. However, this lactic acid bacterium can substitute deoxyribosides or deoxynucleotides (known as an alkali-resistant factor) for cobalamin. Therefore, cobalamin contents detd. by this microbiol. assay are often incorrect in some foods. The difficulty of evaluating whether certain foods contain cobalamin or inactive corrinoids (or both) may be easily resolved by the use of bioautog. with a cobalamin-dependent Escherichia coli after sepn. of the sample by silica gel TLC. LC/electrospray ionization-tandem mass spectrometry is also used to analyze corrinoid compds., and various inactive corrinoid compds. have been identified in foods.
- 22Derevenkov, I. A.; Salnikov, D. S.; Makarov, S. V.; Boss, G. R.; Koifman, O. I. Kinetics and mechanism of oxidation of super-reduced cobalamin and cobinamide by thiosulfate, sulfite and dithionite. Dalton Trans. 2013, 42, 15307– 15316, DOI: 10.1039/c3dt51714dThere is no corresponding record for this reference.
- 23Farquharson, J.; Adams, J. F. The forms of vitamin B12 in foods. Br. J. Nutr. 1976, 36, 127– 136, DOI: 10.1079/BJN1976006323The forms of vitamin B12 in foodsFarquharson, J.; Adams, J. F.British Journal of Nutrition (1976), 36 (1), 127-36CODEN: BJNUAV; ISSN:0007-1145.Vitamin B12 in the forms of sulfitocobalamin [15671-27-9], hydrocobalamin [13422-51-0], methylcobalamin [13422-55-4], cyanocobalamin [68-19-9], and adenosylcobalamin [13870-90-1] was detected in 23 items of food prepd. for consumption. Intestinal absorption of sulfitocobalamin was lower than that of cyanocobalamin in 9 subjects.
- 24Abu-Soud, H. M.; Maitra, D.; Byun, J.; Souza, C. E. A.; Banejee, J.; Saed, G. M.; Diamond, M. P.; Andreana, P. R.; Pennathur, S. The reaction of HOCl and cyanocobalamin: Corrin destruction and the liberation of cyanogen chloride. Free Radical Biol. Med. 2012, 52, 616– 625, DOI: 10.1016/j.freeradbiomed.2011.10.49624The reaction of HOCl and cyanocobalamin: Corrin destruction and the liberation of cyanogen chlorideAbu-Soud, Husam M.; Maitra, Dhiman; Byun, Jaeman; Souza, Carlos Eduardo A.; Banerjee, Jashoman; Saed, Ghassan M.; Diamond, Michael P.; Andreana, Peter R.; Pennathur, SubramaniamFree Radical Biology & Medicine (2012), 52 (3), 616-625CODEN: FRBMEH; ISSN:0891-5849. (Elsevier B.V.)Overprodn. of hypochlorous acid (HOCl) has been assocd. with the development of a variety of disorders such as inflammation, heart disease, pulmonary fibrosis, and cancer through its ability to modify various biomols. HOCl is a potent oxidant generated by the myeloperoxidase-hydrogen peroxide-chloride system. Recently, we have provided evidence to support the important link between higher levels of HOCl and heme destruction and free iron release from Hb and RBCs. Our current findings extend this work and show the ability of HOCl to mediate the destruction of metal-ion derivs. of tetrapyrrole macrocyclic rings, such as cyanocobalamin (Cobl), a common pharmacol. form of vitamin B12. Cyanocobalamin is a water-sol. vitamin that plays an essential role as an enzyme cofactor and antioxidant, modulating nucleic acid metab. and gene regulation. It is widely used as a therapeutic agent and supplement, because of its efficacy and stability. In this report, we demonstrate that although Cobl can be an excellent antioxidant, exposure to high levels of HOCl can overcome the beneficial effects of Cobl and generate proinflammatory reaction products. Our rapid kinetic, HPLC, and mass spectrometric analyses showed that HOCl can mediate corrin ring destruction and liberate cyanogen chloride (CNCl) through a mechanism that initially involves α-axial ligand replacement in Cobl to form a chlorinated deriv., hydrolysis, and cleavage of the phosphonucleotide moiety. Addnl., it can liberate free Co, which can perpetuate metal-ion-induced oxidant stress. Taken together, these results are the first report of the generation of toxic mol. products through the interaction of Cobl with HOCl.
- 25Maita, D.; Byun, J.; Andreana, P. R.; Abdulhamid, I.; Saed, G. M.; Diamond, M. P.; Pennathur, S.; Abu-Soud, H. M. Mechanism of hypochlorous acid-mediated heme destruction and free iron release. Free Radical Biol. Med. 2011, 51, 364– 373, DOI: 10.1016/j.freeradbiomed.2011.03.040There is no corresponding record for this reference.
- 26Teng, F.; Bito, T.; Takenaka, S.; Yabuta, Y.; Watanabe, F. Yoke of the century egg (Pidan) contains a readily digestible form of free vitamin B12. J. Nutr. Sci. Vitaminol. 2016, 62, 366– 371, DOI: 10.3177/jnsv.62.36626Yolk of the century egg (pidan) contains a readily digestible form of free vitamin B12Teng, Fei; Bito, Tomohiro; Takenaka, Shigeo; Yabuta, Yukinori; Watanabe, FumioJournal of Nutritional Science and Vitaminology (2016), 62 (5), 366-371CODEN: JNSVA5; ISSN:0301-4800. (Center for Academic Publications Japan)In this study, we detd. the vitamin B12 content of com. available century eggs (pidan) and characterized their vitamin B12 compns. in detail. The egg yolk and white of century eggs (each 100 g wet wt.) contained 1.9 ± 0.6 and 0.8 ± 0.3 μg of vitamin B12, resp. The vitamin B12 compds. purified from the egg yolk and white were identified as vitamin B12 using liq. chromatog.-electrospray ionization/tandem mass spectrometry. The vitamin B12 present in the yolk or white of century eggs was recovered completely in macromol. fractions, but not in free vitamin B12 fractions by Sephadex G-50 gel filtration. However, with respect to the vitamin B12 bound to protein in the century egg yolk, approx. 52% of the free vitamin B12 was formed during in vitro gastric digestion and no free vitamin B12 was detected in the egg white.
- 27Baik, H. W.; Russell, R. M. Vitamin B12 deficiency in the elderly. Annu. Rev. Nutr. 1999, 19, 357– 377, DOI: 10.1146/annurev.nutr.19.1.35727Vitamin B12 deficiency in the elderlyBaik, H. W.; Russell, R. M.Annual Review of Nutrition (1999), 19 (), 357-377CODEN: ARNTD8; ISSN:0199-9885. (Annual Reviews Inc.)A review with 153 refs. Vitamin B12 deficiency affects 10-15% people over the age of 60, and the lab. diagnosis is usually based on low blood serum vitamin B12 levels or elevated serum methylmalonic acid and homocysteine levels. Although elderly people with low vitamin B12 status frequently lack the classical signs and symptoms of vitamin B12 deficiency (megaloblastic anemia), precise evaluation and treatment in this population is important. Absorption of cryst. vitamin B12 does not decline with advancing age. Compared with the younger population, the absorption of protein-bound vitamin B12 is decreased in the elderly due to a high prevalence of atrophic gastritis in this age group. Atrophic gastritis results in a low acid-pepsin secretion by the gastric mucosa, which in turn decreases the release of free vitamin B12 from food proteins. Hypochlorhydria in atrophic gastritis results in bacterial overgrowth in the stomach and small intestine, and the bacteria may bind vitamin B12 for their own use. The ability to absorb cryst. vitamin B12 remains intact in older people with atrophic gastritis. The 1998 recommended daily allowance for vitamin B12 is 2.4 μg, but elderly people should try to obtain their vitamin B12 from supplements or fortified foods (e.g. fortified ready-to-eat breakfast cereals) to ensure adequate absorption from the gastrointestinal tract. Because the American food supply is now being fortified with folic acid, concern is increasing about neurol. exacerbation in individuals with marginal vitamin B12 status and high-dose folate intake.
- 28Malech, H. L.; Gallin, J. I. Neutrophils in human diseases. N. Engl. J. Med. 1987, 317, 687– 694, DOI: 10.1056/NEJM19870910317110728Current concepts: immunology. Neutrophils in human diseasesMalech H L; Gallin J IThe New England journal of medicine (1987), 317 (11), 687-94 ISSN:0028-4793.There is no expanded citation for this reference.
- 29Chapman, A. L.; Winterbourn, C. C.; Brennan, S. O.; Jordan, T. W.; Kettle, A. J. Characterization of non-covalent oligomers of proteins treated with hypochlorous acid. Biochem. J. 2003, 375, 33– 40, DOI: 10.1042/bj2003068529Characterization of non-covalent oligomers of proteins treated with hypochlorous acidChapman, Anna L. P.; Winterbourn, Christine C.; Brennan, Stephen O.; Jordan, T. William; Kettle, Anthony J.Biochemical Journal (2003), 375 (1), 33-40CODEN: BIJOAK; ISSN:0264-6021. (Portland Press Ltd.)Hypochlorous acid (HOCl) is a potent oxidant produced by myeloperoxidase that causes aggregation of many proteins. Treatment of apoHb and apomyoglobin with HOCl produced a regular series of oligomer bands when the proteins were sepd. by SDS-PAGE under reducing conditions. Aggregation was detectable at a HOCl/protein molar ratio of 0.5:1 and was maximal at ratios of 10:1-20:1. Dimers formed within 1 min of adding HOCl, and further aggregation occurred over the next 30 min. No convincing evidence for covalent crosslinking was obtained by amino acid anal., peptide anal. or electrospray ionization-MS of HOCl-modified apomyoglobin. The latter showed an increase in mass consistent with conversion of the two methionine residues into sulfoxides. A 5-fold excess of HOCl generated approx. three chloramines on the apomyoglobin. These underwent slow decay. Protein carbonyls were formed and were almost entirely located only on the polymer bands. Conversion of pos. into neg. charged groups on the protein by succinylation caused preformed aggregates to dissoc. Treatment of apomyoglobin with taurine chloramine generated methionine sulfoxides but few protein carbonyls, and did not result in aggregation. We conclude that aggregation was due to strong, non-covalent interactions between protein chains. We propose that formation of protein carbonyls and possibly chloramines, along with methionine oxidn., alters protein folding to expose hydrophobic areas on neighboring mols. that assoc. to form dimers and higher-mol.-mass aggregates. This process could lead to the formation of aggregated proteins at sites of myeloperoxidase activity and contribute to inflammatory tissue injury.
- 30Scheuring, E. M.; Sagi, I.; Chance, M. R. Sulur-containing cobalamins: X-ray absorption spectroscopic characterization. Biochemistry 1994, 33, 6310– 6315, DOI: 10.1021/bi00186a03430Sulfur-Containing Cobalamins: X-ray Absorption Spectroscopic CharacterizationScheuring, Eva M.; Sagi, Irit; Chance, Mark R.Biochemistry (1994), 33 (20), 6310-15CODEN: BICHAW; ISSN:0006-2960.Sulfur-contg. cobalamins are thought to have a special role in the intracellular conversion of cyanocobalamin to its coenzyme forms through a Co(I) intermediate. Glutathionylcobalamin is esp. interesting as a possible precursor of cobalamin coenzymes [Wagner et al. (1969) Ann. N.Y.Acad. Sci. 112, 580; Pezacka et al. (1990) Biochem. Biophys. Res. Commun. 169, 443]. Recent NMR data [Brown et al. (1993) Biochem. 32, 8421] strongly support the hypothesis that glutathione coordinates to the cobalt through the sulfur atom in glutathionylcobalamin. In this study three-sulfur contg. cobalamin derivs.(glutathionylcobalamin, sulfitocobalamin, and cysteinylcobalamin) have been characterized by X-ray absorption spectroscopy. The authors give evidence for the sulfur coordination in these compds. and present the corresponding structural information. The Co-Neq distances in the sulfur-contg. cobalamins are very close to one another (1.90 ± 0.01 Å). The Co-S and Co-Nax distances are also similar (Co-S: 2.28-2.35Å and Co-Nax: 2.13-2.16 6 Å) and in the expected range. The X-ray edge positions for the sulfur derivs. shift to lower energies with respect to cyanocobalamin. This indicates strong electron donation from the sulfur to the cobalt and suggests that the effective charge on the cobalt ion in sulfur cobalamins is largely reduced from +3.
- 31Pezacka, E.; Green, R.; Jacobsen, D. W. Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymes. Biochem. Biophys. Res. Commun. 1990, 169, 443– 450, DOI: 10.1016/0006-291X(90)90351-M31Glutathionylcobalamin as an intermediate in the formation of cobalamin coenzymesPezacka, Ewa; Green, Ralph; Jacobsen, Donald W.Biochemical and Biophysical Research Communications (1990), 169 (2), 443-50CODEN: BBRCA9; ISSN:0006-291X.To evaluate the possible role of glutathionylcobalamin (GS-Cbl) in the intracellular metab. of cobalamin, the following reactions were analyzed using exts. of rabbit spleen: (1) decyanation of cyanocobalamin; (2) utilization of GS-Cbl by cobalamin reductase; (3) participation of GS-Cbl in methionine biosynthesis; and (4) conversion of GS-Cbl to adensoylcobalamin. Decyanation of cyanocobalamin required reduced glutathione which appeared to form a complex with the cobalamin. This complex decompd. during the extn. steps to sulfitocobalamin which was identified by HPLC. Cobalamin reductase in spleen ext. was more active with GS-Cbl than with aquocobalamin or cyanocobalamin as substrates (specific activities: 10.4, 2.8, and 0.93 nmol/mg/min, resp.). Methionine synthase utilized GS-Cbl as cofactor more efficiently than aquocobalamin or cyanocobalamin based on initial rates of enzyme activity. This suggests that GS-Cbl is a more direct precursor of the coenzyme required for methionine synthase. Formation of adenosylcobalamin from GS-Cbl was 4-times greater than from aquocobalamin alone. Based on these results, it is proposed that GS-Cbl or a closely related thiol-cobalamin adduct is a proximal precursor in cobalamin coenzyme biosynthesis.