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

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 fa...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1988-11, Vol.104 (5), p.681-682
Main Authors: Nishio, Toshiyuki, Kamimura, Minoru, Murata, Masakazu, Terao, Yoshiyasu, Achiwa, Kazuo
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Esterification
Fundamental and applied biological sciences. Psychology
Hydrolases
Lipase - metabolism
Pseudomonas - enzymology
Pseudomonas fragi
Substrate Specificity
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Summary: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 α-terpineol did not react at all. The lipase exhibited stereoselectivity in the esterification of alcohols such as 2-octanol.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122532