ADSORPTION OF VARIOUS ENZYMES ONTO TALCS SCOPE AND LIMITATIONS OF THIS NEW IMMOBILIZATION SYSTEM

被引：4

作者：

ARSEGUEL, D ^{[1
]}

BABOULENE, M ^{[1
]}

机构：

[1] UNIV TOULOUSE 3,IMRCP LAB,CNRS,UA 470,F-31062 TOULOUSE,FRANCE

来源：

BIOCATALYSIS AND BIOTRANSFORMATION | 1995年 / 12卷 / 04期

关键词：

HORSERADISH PEROXIDASE; PROTEASE; LIPASE; TALC; ADSORPTION; ENZYMATIC ACTIVITY;

D O I：

10.3109/10242429509003189

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：

The adsorption of various enzymes (proteases, lipases and peroxidases) onto the surface of talc (a hydrophobic support) and non-talc materials was investigated. In general, adsorption was favored by the hydrophobicity of the support. We found little evidence for the ionic interactions that characterize adsorption onto mineral supports (clays, porous glasses). Modification of the hydrophobic-hydrophilic balance of the talc support produced new immobilized biocatalysts with high enzyme activity (both lipases and horseradish peroxidase). This represents the first example of this type of talc-protein interaction.

引用

页码：267 / 279

页数：13

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