Characterization of sol-gel bioencapsulates for ester hydrolysis and synthesis

Candida rugosa lipase was entrapped in silica sol-gel particles prepared by hydrolysis of methyltrimethoxysilane and assayed by p-nitrophenyl palmitate hydrolysis, as a function of pH and temperature, giving pH optima of 7.8 (free enzyme) and 5.0-8.0 (immobilized enzyme). The optimum temperature for...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology Vol. 121-124; no. 1-3; pp. 845 - 859
Main Authors: Soares, Cleide M F, de Castro, Heizir F, Itako, Juliana E, de Moraes, Flavio F, Zanin, Gisella M
Format: Journal Article
Language:English
Published: United States Springer Nature B.V 2005
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Summary:Candida rugosa lipase was entrapped in silica sol-gel particles prepared by hydrolysis of methyltrimethoxysilane and assayed by p-nitrophenyl palmitate hydrolysis, as a function of pH and temperature, giving pH optima of 7.8 (free enzyme) and 5.0-8.0 (immobilized enzyme). The optimum temperature for the immobilized enzyme (50-55 degrees C) was 19 degrees C higher than for the free enzyme. Thermal, operational, and storage stability were determined with n-butanol and butyric acid, giving at 45 degrees C a half-life 2.7 times greater for the immobilized enzyme; storage time was 21 d at room temperature. For ester synthesis, the optimum temperature was 47 degrees C, and high esterification conversions were obtained under repeated batch cycles (half-life of 138 h).
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ISSN:0273-2289
0273-2289
1559-0291
DOI:10.1385/ABAB:123:1-3:0845