Modification of lipases with poly(ethylene glycol) and poly(oxyethylene) detergents and their catalytic activities in organic solvents

The α-chymotrypsin-poly(ethylene glycol) complex, which was prepared by lyophilizing an aqueous solution, was found to have high catalytic activity in organic media even when the molar ratio of polymer/enzyme in its preparation stage is unity. In this study, we obtained freeze-dried complexes of lip...

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Bibliographic Details
Published in:Journal of bioscience and bioengineering 2001, Vol.92 (6), p.539-543
Main Authors: Mine, Yurie, Fukunaga, Kimitoshi, Yoshimoto, Makoto, Nakao, Katsumi, Sugimura, Yoshiaki
Format: Article
Language:English
Subjects:
BACTERIA
CANDIDA RUGOSA
detergent-enzyme complex
ENZYME ACTIVITY
enzyme modification
ETHYLENE GLYCOL
lipases
nonaqueous enzymology
PSEUDOMONAS CEPACIA
SOLVENTS
SURFACTANTS
TRIACYLGLYCEROL LIPASE
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Summary:The α-chymotrypsin-poly(ethylene glycol) complex, which was prepared by lyophilizing an aqueous solution, was found to have high catalytic activity in organic media even when the molar ratio of polymer/enzyme in its preparation stage is unity. In this study, we obtained freeze-dried complexes of lipases and poly(ethylene glycol) or poly(oxyethylene) detergents including newly synthesized gemini-type detergents, and their transesterification activity in organic solvents was evaluated. The freeze-dried lipase from Pseudomonas cepacia prepared by using each modifier showed enhanced transesterification activity, exhibiting a similar dependence on the concentration of the modifier in the preparation stage to that of the α-chymotrypsin-poly(ethylene glycol) complex; in contrasts, the one from Candida rugosa did not do so.
ISSN:1389-1723
1347-4421
DOI:10.1016/S1389-1723(01)80312-1