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Enzymatic transesterification with the lipase from Pseudomonas fragi 22.39 B in a non-aqueous reaction system
T Nishio1, M Kamimura, M Murata
1Research & Development Laboratories, Sapporo Breweries, Ltd., Shizuoka.
Journal of Biochemistry
|November 1, 1988
Abstract:
The lipase from Pseudomonas fragi 22.39 B catalyzed the transesterification in ester and alcohol mixtures without any other solvent. Activated esters, such as vinyl and phenyl esters, were excellent acyl donors for the reaction, and the activity was enhanced by increasing the carbon number of the fatty acid fraction of the esters. Primary alcohols were esterified faster than secondary ones in this reaction system, while tertiary alcohols such as alpha-terpineol did not react at all. The lipase exhibited stereoselectivity in the esterification of alcohols such as 2-octanol.