Concanavalin a immobilized affinity adsorbents for reversible use in yeast invertase adsorption

被引：33

作者：

Yavuz, H

Akgöl, S

Arica, Y

Denizli, A ^{[1
]}

机构：

[1] Hacettepe Univ, Dept Chem, TR-06532 Ankara, Turkey

[2] Kirikkale Univ, Dept Biol, Ankara, Turkey

来源：

MACROMOLECULAR BIOSCIENCE | 2004年 / 4卷 / 07期

关键词：

concanavalin A; enzyme immobilization; glycoenzyme; immobilization; invertase; sucrose hydrolysis;

D O I：

10.1002/mabi.200400028

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：

Concanavalin A (Con A) immobilized poly(2-hydroxyethyl methacrylate) (PHEMA) beads were investigated for specific adsorption of yeast invertase from aqueous solutions. PHEMA beads were prepared by a suspension polymerization technique with an average size of 150-200 mum, and activated by epichlorohydrin. Con A was then immobilized by covalent binding onto these beads. The maximum Con A immobilization was found to be 10 mg/g. The invertase-loading capability of the PHEMA/Con A beads was observed at pH 5.0. The values of the Michaelis constant K-m of invertase were significanly larger upon adsorption, indicating decreased smaller for the adsorbed invertase. Adsorption improved the pH stability of the enzyme activity was found to be quite stable in repeated experiments.

引用

页码：674 / 679

页数：6

共 19 条

[1] Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres [J].