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Updated: Apr 12, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026
Production of optically pure L-phenyllactic acid by using engineered Escherichia coli coexpressing L-lactate
Zhaojuan Zheng1, Mingyue Zhao2, Ying Zang2
1College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, People's Republic of China; Jiangsu Key Lab of Biomass-based Green Fuels and Chemicals, Nanjing 210037, People's Republic of China.
Abstract:
L-Phenyllactic acid (L-PLA) is a novel antiseptic agent with broad and effective antimicrobial activity. In addition, L-PLA has been used for synthesis of poly(phenyllactic acid)s, which exhibits better mechanical properties than poly(lactic acid)s. However, the concentration and optical purity of L-PLA produced by native microbes was rather low. An NAD-dependent L-lactate dehydrogenase (L-nLDH) from Bacillus coagulans NL01 was confirmed to have a good ability to produce L-PLA from phenylpyruvic acid (PPA). In the present study, l-nLDH gene and formate dehydrogenase gene were heterologously coexpressed in Escherichia coli. Through two coupled reactions, 79.6mM l-PLA was produced from 82.8mM PPA in 40min and the enantiomeric excess value of L-PLA was high (>99%). Therefore, this process suggested a promising alternative for the production of chiral l-PLA.
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