STABILIZATION OF POTATO-TUBER LIPOXYGENASE ON TALC

被引:14
作者
BATTU, S
COOKMOREAU, J
BENEYTOUT, JL
机构
[1] U.R.A. CNRS No. 1485, Faculté de Médecine et de Pharmacie de Limoges, 87025 Limoges Cedex, 2, Rue du Docteur Marcland
来源
BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM | 1994年 / 1211卷 / 03期
关键词
POTATO TUBER LIPOXYGENASE; ENZYME ADSORPTION; TALC;
D O I
10.1016/0005-2760(94)90150-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Potato tuber lipoxygenase, like many plant enzymes is a very labile protein and can lose activity during or after the purification procedure. In order to overcome this problem, we immobilized potato tuber lipoxygenase by adsorption on talc, a silicate support. Lipoxygenase adsorption greatly increased the long-term stability of the enzyme without modifying enzyme specificity. Moreover, adsorption on talc could be used to purify labile enzymes whose enzymatic activity decreases rapidly during purification stages. A multi-step reaction to produce large quantities (around 100 mg) of fatty acid hydroperoxides without enzyme inactivation was developed.
引用
收藏
页码:270 / 276
页数:7
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