Enzyme immobilization in reactive nanoparticles produced by inverse microemulsion polymerization

被引：43

作者：

Daubresse, C ^{[1
]}

Grandfils, C ^{[1
]}

Jerome, R ^{[1
]}

Teyssie, P ^{[1
]}

机构：

[1] UNIV LIEGE,CERM,INST CHEM,B-4000 LIEGE,BELGIUM

来源：

COLLOID AND POLYMER SCIENCE | 1996年 / 274卷 / 05期

关键词：

inverse microemulsion polymerization; microemulsion; protein immobilization; latex; surface modification;

D O I：

10.1007/BF00652472

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

This paper deals with the immobilization of alkaline phosphatase by physical entrapment within colloidal particles produced by inverse microemulsion polymerization. Functionality has been imparted to the nanoparticle surface by copolymerization of acrylamide (the main monomer), N,N'-methylene-bisacrylamide (the cross-linking agent) with either N-acryloyl-1,6-diaminohexane (an amine promoter) or acrylic acid (a carboxylic acid promoter). The effect of the functional comonomers on the size and zeta potential of the reactive latexes has been studied. Integrity of the immobilized enzyme has been ascertained from its catalytic activity towards hydrolysis of p-nitrophenylphosphate.

引用

页码：482 / 489

页数：8

共 27 条

[1] MICROGELS - MODEL POLYMERS FOR THE CROSS-LINKED STATE [J].