Characterization of CIM monoliths as enzyme reactors

被引：54

作者：

Vodopivec, M

Podgornik, A

Berovic, M

Strancar, A

机构：

[1] BIA Separat, DOO, SI-1000 Ljubljana, Slovenia

[2] Natl Inst Chem, SI-1000 Ljubljana, Slovenia

[3] Univ Ljubljana, Fac Chem & Chem Technol, SI-1000 Ljubljana, Slovenia

来源：

JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2003年 / 795卷 / 01期

关键词：

convective interaction media; monoliths; enzyme reactors; organic acids;

D O I：

10.1016/S1570-0232(03)00551-8

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The immobilization of the enzymes citrate lyase, malate dehydrogenase, isocitrate dehydrogenase and lactate dehydrogenase to CIM monolithic supports was performed. The long-term stability, reproducibility, and linear response range of the immobilized enzyme reactors were investigated along with the determination of the kinetic behavior of the enzymes immobilized on the CIM monoliths. The Michaelis-Menten constant K-m and the turnover number k(3) of the immobilized enzymes were found to be flow-unaffected. Furthermore, the K-m values of the soluble and immobilized enzyme were found to be comparable. Both facts indicate the absence of a diffusional limitation in immobilized CIM enzyme reactors. (C) 2003 Elsevier B.V. All rights reserved.

引用

页码：105 / 113

页数：9

共 47 条

[1] CARRIER MEMBRANE AS A STATIONARY PHASE FOR AFFINITY-CHROMATOGRAPHY AND KINETIC-STUDIES OF MEMBRANE-BOUND ENZYMES [J].