Cloning, Expression, and Characterization of budC Gene Encoding meso-2,3-Butanediol Dehydrogenase from Bacillus licheniformis

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• 作者：Guo-Chao Xu ; Ya-Qian Bian ; Rui-Zhi Han…
• 关键词：Bacillus licheniformis ; meso ; 2 ; 3 ; Butanediol dehydrogenase ; Expression ; Characterization
• 刊名：Applied Biochemistry and Biotechnology
• 出版年：2016
• 出版时间：February 2016
• 年：2016
• 卷：178
• 期：3
• 页码：604-617
• 全文大小：1,023 KB
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• 作者单位：Guo-Chao Xu (1)
  Ya-Qian Bian (1)
  Rui-Zhi Han (1)
  Jin-Jun Dong (1)
  Ye Ni (1)
  
  1. The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, Jiangsu, China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Biochemistry
  
• 出版者：Humana Press Inc.
• ISSN：1559-0291

文摘

The budC gene encoding a meso-2,3-butanediol dehydrogenase (BlBDH) from Bacillus licheniformis was cloned and overexpressed in Escherichia coli BL21(DE3). Sequence analysis reveals that this BlBDH belongs to short-chain dehydrogenase/reductase (SDR) superfamily. In the presence of NADH, BlBDH catalyzes the reduction of diacetyl to (3S)-acetoin (97.3 % ee), and further to (2S,3S)-2,3-butanediol (97.3 % ee and 96.5 % de). Similar to other meso-2,3-BDHs, it shows oxidative activity to racemic 2,3-butanediol whereas no activity toward racemic acetoin in the presence of NAD+. For diacetyl reduction and 2,3-butanediol oxidation, the pH optimum of BlBDH is 5.0 and 10.0, respectively. Unusually, it shows relatively high activity over a wide pH range from 5.0 to 8.0 for racemic acetoin reduction. BlBDH shows lower K _m and higher catalytic efficiency toward racemic acetoin (K _m = 0.47 mM, k _cat /K _m = 432 s–1·mM–1) when compared with 2,3-butanediol (K _m = 7.25 mM, k _cat /K _m = 81.5 s–1·mM–1), indicating its physiological role in favor of reducing racemic acetoin into 2,3-butanediol. The enzymatic characterization of BlBDH provides evidence for the directed engineering of B. licheniformis for producing enantiopure 2,3-butanediol.