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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Published in: | Applied biochemistry and biotechnology Vol. 121-124; no. 1-3; pp. 845 - 859 |
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Main Authors: | , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Springer Nature B.V
2005
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Subjects: | |
Online Access: | Get full text |
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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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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0273-2289 0273-2289 1559-0291 |
DOI: | 10.1385/ABAB:123:1-3:0845 |