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Catalyzed Oxidation of Carotenoids by Lactoperoxidase in the Presence of Ethanol

  • Raheleh Ravanfar
    Raheleh Ravanfar
    Department of Food Science, Cornell University, Ithaca, New York United States
  • Peter Lawrence
    Peter Lawrence
    Department of Food Science, Cornell University, Ithaca, New York United States
  • Kyle Kriner
    Kyle Kriner
    Department of Food Science, Cornell University, Ithaca, New York United States
    More by Kyle Kriner
  • , and 
  • Alireza Abbaspourrad*
    Alireza Abbaspourrad
    Department of Food Science, Cornell University, Ithaca, New York United States
    *E-mail: [email protected]. Phone: 607-255-2923.
Cite this: J. Agric. Food Chem. 2019, 67, 6, 1742–1748
Publication Date (Web):January 24, 2019
https://doi.org/10.1021/acs.jafc.8b06558
Copyright © 2019 American Chemical Society

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    Abstract

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    The discovery of the lactoperoxidase system as a biocatalyst in milk was a landmark finding. The activation of this system using hydrogen peroxide (H2O2) raised hopes for oxidation of various organic substrates. The involvement of lactoperoxidase system in the catalyzed-oxidation of carotenoids in the whey proteins, and the effect of various solvents on carotenoids’ oxidation reaction rate has been studied. However, there is no evidence for this reaction without the addition of oxidizing agents, such as peroxides. Here, we reveal that carotenoids are oxidized through the addition of just ethanol in the presence of lactoperoxidase. The oxidation of carotenoids through this exquisite strategy is ∼360 times faster than harnessing the lactoperoxidase system in whey proteins via the addition of hydrogen peroxide. Bearing in mind that ethanol is not an oxidizing agent, this observation suggests a potential paradigm shift in our understanding of lactoperoxidase and catalyzed oxidation in biochemical systems.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.jafc.8b06558.

    • Figure S1. Schematic of Cheddar cheese production, colored using annatto carotenoids. Figure S2. (a) L* (lightness) and (b) b* (yellowness) values of the colored whey treated with 250 ppm hydrogen peroxide, different ethanol concentrations, and water to correct the dilution factor. Figure S3. Ethanol addition to the annatto carotenoid solution at a pH range of 2–12. Figure S4. The addition of ethanol to annatto carotenoids and casein, indicating a lack of color change and coagulation of casein upon addition of ethanol. Figure S5. The DART-MS spectrum of the annatto, and a proposed structure for its main fragment at 150 m/z. Figure S6. DART-MS spectra of the colored whey proteins treated with a) ethanol (30%, v/v) and b) hydrogen peroxide (250 ppm). Figure S7. DART-MS spectra of the colored whey proteins treated with a) 30% (v/v) ethanol and b) 250 ppm hydrogen peroxide. c) Control, untreated colored whey proteins. Figure S8. Schematic of the lactoperoxidase activity assay. Figure S9. FTIR spectra of the ETW and HTW in comparison with the colored whey control. Table S1. Composition analysis of the colored whey proteins. (PDF)

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    Cited By

    This article is cited by 1 publications.

    1. Raheleh Ravanfar, Alireza Abbaspourrad. Monitoring the heme iron state in horseradish peroxidase to detect ultratrace amounts of hydrogen peroxide in alcohols. RSC Advances 2021, 11 (17) , 9901-9910. https://doi.org/10.1039/D1RA00733E

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