HYDROLYSIS MECHANISM OF TRIOLEIN WITH LIPASA IN MEMBRANE BIOREACTOR USING HOLLOW FIBER

被引:5
作者
GOTO, M [1 ]
GOTO, M [1 ]
NAKASHIO, F [1 ]
YOSHIZUKA, K [1 ]
INOUE, K [1 ]
机构
[1] SAGA UNIV,DEPT APPL CHEM,SAGA 840,JAPAN
关键词
BIOCHEMICAL ENGINEERING; ENZYME REACTION; MEMBRANE BIOREACTOR; HYDROLYSIS; TRIOLEIN; LIPASE; HOLLOW FIBER;
D O I
10.1252/kakoronbunshu.17.477
中图分类号
TQ [化学工业];
学科分类号
0817 ;
摘要
Triolein, a major component of olive oil, was hydrolyzed with lipase in a membrane bioreactor using hollow fiber. The hydrolysis mechanism of triolein was investigated, taking account of the mass transfer of triolein and oleic acid through the membrane. It was made clear that oleic acid, one of the products, strongly inhibited the hydrolysis of triolein at high concentration. Glycerin, another product, did not inhibit the reaction. This hydrolysis reaction with lipase could be quantitatively explained by the Michaelis-Menten mechanism at the interface between the aqueous and organic phases, taking account of the adsorption of lipase and the permeation rate of triolein and oleic acid.
引用
收藏
页码:477 / 483
页数:7
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