Rationally re-designed mutation of NAD-independent l-lactate dehydrogenase: high optical resolution of racemic mandelic acid by the engineered Escherichia coli
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- 作者：Tianyi Jiang (1)
Chao Gao (1)
Peipei Dou (1) (2)
Cuiqing Ma (1)
Jian Kong (1)
Ping Xu (1) (2) - 关键词：NAD ; independent l ; lactate dehydrogenase ; Site ; directed mutagenesis ; Optical resolution ; d ; mandelic acid
- 刊名：Microbial Cell Factories
- 出版年：2012
- 出版时间：December 2012
- 年：2012
- 卷：11
- 期：1
- 全文大小：431KB
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Chao Gao (1)
Peipei Dou (1) (2)
Cuiqing Ma (1)
Jian Kong (1)
Ping Xu (1) (2)
1. State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China
2. State Key Laboratory of Microbial Metabolism and Schoolof Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China - ISSN：1475-2859
文摘
Background NAD-independent l-lactate dehydrogenase (l-iLDH) from Pseudomonas stutzeri SDM can potentially be used for the kinetic resolution of small aliphatic 2-hydroxycarboxylic acids. However, this enzyme showed rather low activity towards aromatic 2-hydroxycarboxylic acids. Results Val-108 of l-iLDH was changed to Ala by rationally site-directed mutagenesis. The l-iLDH mutant exhibited much higher activity than wide-type l-iLDH towards l-mandelate, an aromatic 2-hydroxycarboxylic acid. Using the engineered Escherichia coli expressing the mutant l-iLDH as a biocatalyst, 40 g·L-1 of dl-mandelic acid was converted to 20.1 g·L-1 of d-mandelic acid (enantiomeric purity higher than 99.5%) and 19.3 g·L-1 of benzoylformic acid. Conclusions A new biocatalyst with high catalytic efficiency toward an unnatural substrate was constructed by rationally re-design mutagenesis. Two building block intermediates (optically pure d-mandelic acid and benzoylformic acid) were efficiently produced by the one-pot biotransformation system.