Asymmetric transesterification of secondary alcohols catalyzed by feruloyl esterase from Humicola insolens.
A new asymmetric transesterification of secondary alcohols catalyzed by feruloyl esterase from Humicola insolens has been found. Although alcohols are not the natural substrates for this enzyme, a high R enantioselectivity was observed. Stereochemical studies showed that variations in substrate structure lead to strong variations in enantioselectivity. The highest enantioselectivities are obtained when the beta-carbon of the secondary alcohol is tertiary or quaternary.
Hatzakis
Nikos S
NS
Department of Chemistry, University of Crete, Iraklion 71409, Crete, Greece.
Smonou
Ioulia
I
D000438:Alcohols / Q000737:chemistry* / Q000378:metabolism*; D001203:Ascomycota / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002384:Catalysis; D004951:Esterification; D015394:Molecular Structure; D013379:Substrate Specificity; D013696:Temperature
D000438:Alcohols; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase