Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases

B. K. YANG; J. P. CHEN

doi:10.1111/j.1365-2621.1994.tb06982.x

Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases

B. K. YANG^*, J. P. CHEN

^*Corresponding author for this work

Research output: Contribution to journal › Journal Article › peer-review

16 Scopus citations

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.

Original language	English
Pages (from-to)	424-427
Number of pages	4
Journal	Journal of Food Science
Volume	59
Issue number	2
DOIs	https://doi.org/10.1111/j.1365-2621.1994.tb06982.x
State	Published - 03 1994
Externally published	Yes

Keywords

gel matrix
hydrolysis
lipase
lipolytic
triglycerides

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10.1111/j.1365-2621.1994.tb06982.x

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title = "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.",

keywords = "gel matrix, hydrolysis, lipase, lipolytic, triglycerides",

author = "YANG, {B. K.} and CHEN, {J. P.}",

year = "1994",

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doi = "10.1111/j.1365-2621.1994.tb06982.x",

language = "英语",

volume = "59",

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journal = "Journal of Food Science",

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TY - JOUR

T1 - Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases

AU - YANG, B. K.

AU - CHEN, J. P.

PY - 1994/3

Y1 - 1994/3

N2 - 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.

AB - 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.

KW - gel matrix

KW - hydrolysis

KW - lipase

KW - lipolytic

KW - triglycerides

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U2 - 10.1111/j.1365-2621.1994.tb06982.x

DO - 10.1111/j.1365-2621.1994.tb06982.x

M3 - 文章

AN - SCOPUS:84985181053

SN - 0022-1147

VL - 59

SP - 424

EP - 427

JO - Journal of Food Science

JF - Journal of Food Science

IS - 2

ER -

Gel Matrix Influence on Hydrolysis of Triglycerides by Immobilized Lipases

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