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- W2788330318 abstract "d-Mandelate dehydrogenase (DMDH) has the potential to convert d-mandelic acid to phenylglyoxylic acid (PGA), which is a key building block in the field of chemical synthesis and is widely used to synthesize pharmaceutical intermediates or food additives. A novel NAD+-dependent d-mandelate dehydrogenase was cloned from Lactobacillus harbinensi (LhDMDH) by genome mining and expressed in Escherichia coli BL21. After being purified to homogeneity, the oxidation activity of LhDMDH toward d-mandelic acid was approximately 1200 U·mg-1, which was close to four times the activity of the probe. Meanwhile, the kcat/ Km value of LhDMDH was 28.80 S-1·mM-1, which was distinctly higher than the probe. By coculturing two E. coli strains expressing LhDMDH and LcLDH, we developed a system for the efficient synthesis of PGA, achieving a 60% theoretical yield and 99% purity without adding coenzyme or cosubstrate. Our data supports the implementation of a promising strategy for the chiral resolution of racemic mandelic acid and the biosynthesis of PGA." @default.
- W2788330318 created "2018-03-06" @default.
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- W2788330318 date "2018-02-20" @default.
- W2788330318 modified "2023-09-25" @default.
- W2788330318 title "Biosynthesis of Phenylglyoxylic Acid by LhDMDH, a Novel <scp>d</scp>-Mandelate Dehydrogenase with High Catalytic Activity" @default.
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- W2788330318 doi "https://doi.org/10.1021/acs.jafc.7b05835" @default.
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