Abstract
An NADH-dependent phenylpyruvate reductase (LaPPR) was identified through screening the shotgun library of Lactobacillus sp. CGMCC 9967. It belongs to d-3-phosphoglycerate dehydrogenase (PGDH) subfamily of 2-hydroxy acid dehydrogenase superfamily. LaPPR was stable at pH 6.5 and 30°C, with a half-life of 152h. LaPPR has a substrate preference towards aromatic to aliphatic keto acids, and various keto acids could be reduced into d-hydroxy acids with excellent enantioselectivity (>99%). By construction the coexpression system with glucose dehydrogenase, as much as 100gL−1 phenylpyruvic acid was asymmetrically reduced into d-phenyllactic acid with 91.3% isolation yield and 243gL−1d−1 productivity. The results suggest that LaPPR is a promising biocatalyst for the efficient synthesis of optically pure d-phenyllactic acid.
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