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A Comparison of Lipase-Catalyzed Ester Hydrolysis in Reverse Micelles, Organic Solvents, and Biphasic Systems

A Comparison of Lipase-Catalyzed Ester Hydrolysis in Reverse Micelles, Organic Solvents, and Biphasic Systems

F Yang, A J Russell

Biotechnol Bioeng. 1995 Jul 5;47(1):60-70.

PMID: 18623367

Abstract:

The performance of lipases from Candida rugosa and wheat germ have been investigated in three reaction media using three acetate hydrolyses as model reactions (ethyl acetate, allyl acetate, and prenyl acetate). The effect of substrate properties and water content were studied for each system (organic solvent, biphasic system, and reverse micelles). Not unexpectedly, the effect of water content is distinct for each system, and the optimal water content for enzyme activity is not always the same as that for productivity. A theoretical model has been used to simulate and predict enzyme performance in reverse micelles, and a proposed partitioning model for biphasic systems agrees well with experimental results. While the highest activities observed were in the micellar system, productivity in microemulsions is limited by low enzyme concentrations. Biphasic systems, however, support relatively good activity and productivity. The addition of water to dry organic solvents, combined with the dispersion of lyophilized enzyme powders in the solvent, resulted in significant enzyme aggregation, which not surprisingly limits the applicability of the "anhydrous" enzyme suspension approach. (c) 1995 John Wiley & Sons, Inc.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1191168	Prenyl acetate		1191-16-8	Price

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