Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases |
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| Authors: | B. K. YANG J. P. CHEN |
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| Affiliation: | Author Yang, formerly with the Center for Dairy Research, Univ. of Wisconsin-Madison, is now with the Dept. of Food Science &Animal Industries, Alabama A &M Univ., P.O. Box 264, Normal, AL 35762. Author Chen's present address: Dept. of Chemical Engineering, National Chung Kung Univ., Taiwan. Address inauiries to Dr. Baokang Yang. |
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| 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. |
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| Keywords: | lipase lipolytic gel matrix hydrolysis triglycerides |
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