Journal
BIOTECHNOLOGY LETTERS
Volume 39, Issue 11, Pages 1741-1746Publisher
SPRINGER
DOI: 10.1007/s10529-017-2415-1
Keywords
Asymmetric reduction; Carbonyl reductase; Coenzyme regeneration; Ketopantolactone; (R)-Pantolactone; Saccharomyces cerevisiae; Spontaneous hydrolysis
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Funding
- Natural Science Foundation of Zhejiang Province, China [LY17B020012, LQ16C020003, LQ14C010002]
- Xinmiao Talents Program of Zhejiang Province [2016R403074]
- National Natural Science Foundation of China [21405140, 31600181]
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To characterize a recombinant carbonyl reductase from Saccharomyces cerevisiae (SceCPR1) and explore its use in asymmetric synthesis of (R)-pantolactone [(R)-PL]. The NADPH-dependent SceCPR1 exhibited strict (R)-enantioselectivity and high activity in the asymmetric reduction of ketopantolactone (KPL) to (R)-PL. Escherichia coli, coexpressing SceCPR1 and glucose dehydrogenase from Exiguobacterium sibiricum (EsGDH), was constructed to fulfill efficient NADPH regeneration. During the whole-cell catalyzed asymmetric reduction of KPL, the spontaneous hydrolysis of KPL significantly affected the yield of (R)-PL, which was effectively alleviated by the employment of the substrate constant-feeding strategy. The established whole-cell bioreduction for 6 h afforded 458 mM (R)-PL with the enantiomeric excess value of > 99.9% and the yield of 91.6%. Escherichia coli coexpressing SceCPR1 and EsGDH efficiently catalyzed the asymmetric synthesis of (R)-PL through the substrate constant-feeding strategy.
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