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Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases

Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases ABSTRACT The hydrolytic activities and specificities of gel‐entrapped C. cylindracae lipase (CCL) and R. arrhizus lipase (RAL) toward olive oil and tributyrin were investigated. Lipases in hydrophobic gels with the longest chain lengths generally displayed highest activity. The optimal temperature was 30–35° for free and 37–40° for gel‐entrapped lipases. The ratio of the activity on tributyrin to that of olive oil (expressed as T/O ratio), an indicator of substrate specificity, increased from 0.3 for free lipases to 12.3 ± 2.3 for CCL lipase in ENTP‐2000‐formed gel and 16.2 ± 0.3 for RAL lipase in ENTP‐4000‐formed gel. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases

Journal of Food Science , Volume 59 (2) – Mar 1, 1994

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References (30)

Publisher
Wiley
Copyright
Copyright © 1994 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
DOI
10.1111/j.1365-2621.1994.tb06982.x
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT The hydrolytic activities and specificities of gel‐entrapped C. cylindracae lipase (CCL) and R. arrhizus lipase (RAL) toward olive oil and tributyrin were investigated. Lipases in hydrophobic gels with the longest chain lengths generally displayed highest activity. The optimal temperature was 30–35° for free and 37–40° for gel‐entrapped lipases. The ratio of the activity on tributyrin to that of olive oil (expressed as T/O ratio), an indicator of substrate specificity, increased from 0.3 for free lipases to 12.3 ± 2.3 for CCL lipase in ENTP‐2000‐formed gel and 16.2 ± 0.3 for RAL lipase in ENTP‐4000‐formed gel.

Journal

Journal of Food ScienceWiley

Published: Mar 1, 1994

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