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Characterization of a Thermostable Cyclodextrin Glucanotransferase Isolated from Bacillus stearothermophilus ET1†
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Hyun-Soo Lee,# Vera A. Spiridonova,
and Kwan-Hwa Park*‡
Section:Abstract
A thermostable cyclodextrin glucanotransferase (CGTase) was isolated from a Bacillus stearothermophilus strain, ET1, which was screened from Korean soil. The corresponding CGTase gene cloned in Escherichia coli shared 84% and 88% identity with CGTase genes from other B. stearothermophilus strains at the nucleotide and amino acid sequence level, respectively. The enzyme was purified to apparent homogeneity by β-cyclodextrin (CD) affinity chromatography and high-performance liquid chromatography. The enzyme had an apparent molecular mass of 66,800 Da and a pI of 5.0. The optimum pH for the enzyme-catalyzed reaction was pH 6.0, and the optimum temperature was observed at 80 °C. Thermostability of the enzyme was enhanced by Ca2+. A 13% (w/v) cornstarch solution was liquefied and converted to CDs solely using this enzyme. The cornstarch conversion rate was 44% and α-, β-, and γ-CDs were produced in the ratio of 4.2:5.9:1.
Keywords: Cyclodextrin glucanotransferase; thermostability; cyclodextrin; Bacillus stearothermophilus
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This article has been cited by 1 ACS Journal articles (1 most recent appear below).
Modulation of Cyclizing Activity and Thermostability of Cyclodextrin Glucanotransferase and Its Application as an Antistaling Enzyme
Sung-Ho Lee, Young-Wan Kim, Suyong Lee, Joong-Hyuck Auh, Sung-Suk Yoo, Tae-Jip Kim, Jung-Wan Kim, Sun-Tae Kim, Hoe-Jin Rho, Jin-Hwan Choi, Young-Bae Kim, and Kwan-Hwa ParkJournal of Agricultural and Food Chemistry2002 50 (6), 1411-1415Modulation of Cyclizing Activity and Thermostability of Cyclodextrin Glucanotransferase and Its Application as an Antistaling Enzyme
Sung-Ho Lee, Young-Wan Kim, Suyong Lee, Joong-Hyuck Auh, Sung-Suk Yoo, Tae-Jip Kim, Jung-Wan Kim, Sun-Tae Kim, Hoe-Jin Rho, Jin-Hwan Choi, Young-Bae Kim, and Kwan-Hwa ParkJournal of Agricultural and Food Chemistry2002 50 (6), 1411-1415Cyclodextrin glucanotransferase from Bacillus stearothermophilus ET1 (CGTase ET1) is a potential antistaling enzyme with cyclodextrin (CD)-forming activity. To reduce cyclization activity of CGTase ET1, phenylalanine residues at 191 and 255 were replaced ...
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History
- Published In Issue March 16, 1998
- Received for review August 14, 1997. Revised manuscript received December 1, 1997. Accepted December 7, 1997. Part of this work was supported by Research Center for New-Bio materials in Agriculture and by the Korean Science and Engi neering Foundation. We also thank Samyang Genex (Korea) for financial support.
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