Enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus

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• 作者：Yibo Zhu ; Fagen Hu ; Yingyue Zhu ; Limei Wang ; Bin Qi
• 关键词：d ; Lactate dehydrogenase ; 3 ; Phenyllactic acid ; Phenylpyruvic acid ; Recognition site residue replacement ; Whole ; cell transformation
• 刊名：Biotechnology Letters
• 出版年：2015
• 出版时间：June 2015
• 年：2015
• 卷：37
• 期：6
• 页码：1233-1241
• 全文大小：737 KB
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• 作者单位：Yibo Zhu (1) (2)
  Fagen Hu (1) (2) (3)
  Yingyue Zhu (1) (2)
  Limei Wang (1) (2)
  Bin Qi (1) (2)
  
  1. School of Biotechnology and Food Engineering, Changshu Institute of Technology, Changshu, 215500, Jiangsu, People’s Republic of China
  2. Key Laboratory of Food and Biotechnology of Suzhou, Changshu Institute of Technology, Changshu, 215500, Jiangsu, People’s Republic of China
  3. School of Biology and Basic Medical Sciences, Soochow University, Suzhou, 215123, Jiangsu, People’s Republic of China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Microbiology
  Biotechnology
  Applied Microbiology
  Biochemistry
  
• 出版者：Springer Netherlands
• ISSN：1573-6776

文摘

Objectives The Tyr52 residue of d-lactate dehydrogenase (d-LDH) from Lactobacillus pentosus was replaced with small hydrophobic residues and overexpressed in E. coli BL21 (DE3) to enhance 3-phenyllactic acid (PLA) synthesis by whole-cell catalyst. Results Escherichia coli pET-28a-d-ldh produced 12.2?g PLA l? in 3?h, with a molar conversion rate of 61?%, while E. coli pET-28a-d-ldh Y52V produced 15.6?g PLA l?, with a molar conversion rate of 77?%. This study demonstrates the feasibility of using engineered E. coli for PLA production from phenylpyruvate (PPA) and showed that site-directed mutagenesis of d-ldh markedly improved PLA yield and substrate conversion rate. Conclusion This biocatalytic system is a promising platform for PLA production from PPA.