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Characterization of a d ‐Lactate Dehydrogenase from Lactobacillus fermentum JN248 with High Phenylpyruvate Reductive Activity
Author(s) -
Chen Lixia,
Bai Yajun,
Fan TaiPing,
Zheng Xiaohui,
Cai Yujie
Publication year - 2017
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/1750-3841.13863
Subject(s) - lactobacillus fermentum , lactate dehydrogenase , chemistry , biocatalysis , antimicrobial , lactic acid , enzyme , biochemistry , dehydrogenase , lactobacillaceae , catalysis , bacteria , nuclear chemistry , lactobacillus , biology , organic chemistry , fermentation , genetics , ionic liquid , lactobacillus plantarum
Phenyllactic acid (PLA) is a novel antimicrobial compound. A novel NADH‐dependent d ‐lactate dehydrogenase ( d ‐LDH), named as LF‐ d ‐LDH0653, with high phenylpyruvate (PPA) reducing activity was isolated from Lactobacillus fermentum JN248. Its optimum pH and temperature were 8.0 and 50 °C, respectively. The Michaelis–Menten constant ( K m ), turnover number ( k cat ), and catalytic efficiency ( k cat / K m ) for NADH were 1.20 mmol/L, 67.39 s −1 , and 56.16 (mmol/L) −1 s −1 , respectively. The ( K m ), ( k cat ), and ( k cat / K m ) for phenylpyruvate were 1.68 mmol/L, 122.66 s −1 , and 73.01 (mmol/L) −1 s −1 , respectively. This enzyme can catalyze phenylpyruvate and the product presented excellent optical purity (enantioselectivity >99%). The results suggest that LF‐ d ‐LDH0653 is a promising biocatalyst for the efficient synthesis of optically pure d ‐PLA. Practical Application A novel d ‐LDH with phenylpyruvate reducing activity has been isolated and identified. It could be used as a reference for improving the production of optically pure d ‐PLA. d ‐PLA has a potential for application as antimicrobial an agent in dairy industry and baking industry, pharmaceutical agent in medicine and cosmetics.