Oleate Hydratase from Lactobacillus rhamnosus ATCC 53103: A FADH2-Dependent Enzyme with Remarkable Industrial Potential
نویسندگان
چکیده
Recently, we described the preparation of recombinant oleate hydratase from Lactobacillus rhamnosus ATCC 53103. We observed that purified C-terminal His-tagged enzyme was completely inactive and catalytic activity partially restored only in presence a large amount flavin adenine dinucleotide (FAD). In present work, assess this reduced form (FADH2) is at least one hundred times as active same concentration FAD. By means two different biochemical processes, demonstrated unambiguously 53103 FADH2-dependent enzyme. As first relevant application discovery, devised preparative procedure for stereoselective synthesis (R)-10-hydroxystearic acid. Accordingly, hydration oleic acid (up to 50 g/L) performed on multigram scale using FADH2 generated situ cofactor. The produced (ee > 97%) precipitates reaction solvent (water/glycerol/ethanol) conveniently recovered by simple filtration (>90% yield).
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ژورنال
عنوان ژورنال: Catalysts
سال: 2021
ISSN: ['2073-4344']
DOI: https://doi.org/10.3390/catal11091051