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J. Biochem, 1988, Vol. 104, No. 5 681-682
© 1988 Japanese Biochemical Society

other

Enzymatic Transesterification with the Lipase from Pseudomonas fragi 22.39 B in a Non-Aqueous Reaction System

Toshiyuki Nishio*, Minoru Kamimura*, Masakazu Murata**, Yoshiyasu Terao** and Kazuo Achiwa**

*Research & Development Laboratories, Sapporo Breweries, Ltd. Yaizu, Shizuokcz 425
**Faculty of Pharmaceutical Sciences, University of Shizuoka Shizuoka, Shizuoka 422

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.


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