黄蛋白
黄素腺嘌呤二核苷酸
化学
生物化学
酶
黄素组
辅因子
立体化学
作者
Stefano Serra,Davide De Simeis,Stefano Marzorati,Mario Valentino
出处
期刊:Catalysts
[MDPI AG]
日期:2021-08-30
卷期号:11 (9): 1051-1051
被引量:7
标识
DOI:10.3390/catal11091051
摘要
Recently, we described the preparation of the recombinant oleate hydratase from Lactobacillus rhamnosus ATCC 53103. We observed that the purified C-terminal His-tagged enzyme was completely inactive and the catalytic activity was partially restored only in presence of a large amount of flavin adenine dinucleotide (FAD). In the present work, we assess that this hydratase in the presence of the reduced form of flavin adenine dinucleotide (FADH2) is at least one hundred times as active as in the presence of the same concentration of FAD. By means of two different biochemical processes, we demonstrated unambiguously that oleate hydratase from Lactobacillus rhamnosus ATCC 53103 is a FADH2-dependent enzyme. As a first relevant application of this discovery, we devised a preparative procedure for the stereoselective synthesis of (R)-10-hydroxystearic acid. Accordingly, the hydration of oleic acid (up to 50 g/L) is performed on a multigram scale using the recombinant hydratase and FADH2 generated in situ as cofactor. The produced (R)-10-hydroxystearic acid (ee > 97%) precipitates from the reaction solvent (water/glycerol/ethanol) and is conveniently recovered by simple filtration (>90% yield).
科研通智能强力驱动
Strongly Powered by AbleSci AI