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 152 h. 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 100 g L(-1) phenylpyruvic acid was asymmetrically reduced into D-phenyllactic acid with 91.3% isolation yield and 243 g L(-1) d(-1) productivity. The results suggest that LaPPR is a promising biocatalyst for the efficient synthesis of optically pure D-phenyllactic acid.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Xu GC,Zhang LL,Ni Ydoi
10.1016/j.jbiotec.2015.12.011subject
Has Abstractpub_date
2016-03-20 00:00:00pages
29-37eissn
0168-1656issn
1873-4863pii
S0168-1656(15)30210-8journal_volume
222pub_type
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journal_title：Journal of biotechnology
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