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
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
收藏
页码:1087 / 1091
页数:5
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