Asymmetric bioreduction of γ-and δ-keto acids by native carbonyl reductases from Saccharomyces cerev

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Optically pure (R)-γ-and (R)-δ-lactones can be prepared by intramolecular cyclization of chiral hydroxy acids/ esters reduced asymmetrically from γ-and δ-keto acids/esters using Saccharomyces cerevisiae (S.cerevisiae) as a whole-cell biocatalyst.However,some of the enzymes catalyzing these reactions in S.cerevisiae are still unknown up to date.In this report,two carbonyl reductases,OdCR1 and OdCR2,were successfully discovered,and cloned from S.cerevisiae using a genome-mining approach,and overexpressed in Escherichia coli (E.coli).Compared with OdCR1,OdCR2 can reduce 4-oxodecanoic acid and 5-oxodecanoic acid asymmetrically with higher stereoselectivity,generating (R)-γ-decalactone (99% ee) and (R)-δ-decalactone (98% ee) in 85% and 92% yields,respectively.This is the first report of native enzymes from S.cerevisiae for the enzymatic synthesis of chiral γ-and δ-lactones which is of wide uses in food and cosmetic industries.
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