Stability and catalytic kinetics of acid phosphatase immobilized on composite beads of chitosan and activated clay

被引：46

作者：

Chang, MY ^{[1
]}

Juang, RS

机构：

[1] Natl United Univ, Dept Chem Engn, Miaoli 360, Taiwan

[2] Yuan Ze Univ, Dept Chem Engn, Chungli 320, Taiwan

来源：

PROCESS BIOCHEMISTRY | 2004年 / 39卷 / 09期

关键词：

acid phosphatase; immobilization; composite beads; chitosan; activated clay; catalytic kinetics; stability;

D O I：

10.1016/S0032-9592(03)00221-8

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 stability of acid phosphatase immobilized on composite beads was studied. The beads were prepared from equal weights of cuttlebone chitosan and activated clay and were cross-linked with glutaraldehyde. The immobilized enzyme maintained 90% of its original activity after 50 times of reuse. The immobilized acid phosphatase revealed acceptable thermal and pH stabilities over a broad experimental range. Thermal deactivation of immobilized enzyme was also examined by first-order kinetics and the deactivation energy was determined. The kinetics of a model reaction catalyzed by the immobilized acid phosphatase was finally investigated by the Michaelis-Menten equation. (C) 2003 Elsevier Ltd. All rights reserved.

引用

页码：1087 / 1091

页数：5

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