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Improving catalytic activity of Lactobacillus harbinensis D-mandelate dehydrogenase toward D-o-chloromandelic acid by laboratory evolution

文献类型： 外文期刊

作者： Tang, Cun-Duo 1 ; Zhang, Xiang 1 ; Shi, Hong-Ling 1 ; Liu, Xin-Xin 1 ; Wang, Hong-Yan 1 ; Lu, Yun-Feng 1 ; Zhang, Si-Pu 4 ; Kan, Yun-Chao 1 ; Yao, Lun-Guang 1 ;

作者机构： 1.Nanyang Normal Univ, Henan Prov Key Lab Funiu Mt Insect Biol, Nanyang 473061, Peoples R China

2.Nanyang Normal Univ, Henan Provincal Engn & Technol Ctr Hlth Prod Lives, Nanyang 473061, Peoples R China

3.Nanyang Normal Univ, Coll Life Sci & Agr Engn, Nanyang 473061, Peoples R China

4.Henan Acad Agr Sci, Zhengzhou 450002, Peoples R China

5.Nanyang Normal Univ, Henan Prov Key Lab Funiu Mt Insect Biol, 1638 Wolong Rd, Nanyang 473061, Henan, Peoples R China

关键词： D -mandelate dehydrogenase; Halogenated compound; Molecular dynamics simulation; Semi -rational design; Laboratory evolution

期刊名称：MOLECULAR CATALYSIS （ 2021影响因子：5.089； 五年影响因子：4.788 ）

ISSN： 2468-8231

年卷期： 2022 年 531 卷

页码：

收录情况： SCI

摘要： In the pharmaceutical and chemical industry, L-o-chlorophenylglycine and its derivatives are very important building blocks. Nevertheless, the catalytic activity of natural D-mandelate dehydrogenase (DMDH) toward D-o- chloromandelic acid (D-o-CMA) was very low, which greatly limits its industrial application. Taking Lactobacillus harbinensisD-mandelate dehydrogenase (LhDMDH) as parent, laboratory evolution was performed to improve its catalytic performance toward D-o-chloromandelic acid. An A59G/N252G mutant of LhDMDH with a higher catalytic performance toward D-o-chloromandelic acid was obtained, its catalytic activity was approximately 8.4 times than that of LhDMDH. Furthermore, the optimal reaction temperature of A59G/N252G is 50 degrees C. Mean-while, the Kcat value toward D-o-CMA of A59G/N252G is 18.33 s-1, which is about 10 times of LhDMDH (1.81 s-1). Lastly, using the in silico design approach, the molecular basis about its catalytic performance improvement was preliminarily explored. Therefore, these researchs established solid practice foundation for the molecular modification of D-mandelate dehydrogenase for catalytic performance.

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