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

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 im...

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Bibliographic Details
Published inProcess biochemistry (1991) Vol. 39; no. 9; pp. 1087 - 1091
Main Authors Chang, Min-Yun, Juang, Ruey-Shin
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 31.05.2004
Subjects
Acid phosphatase
Activated clay
Catalytic kinetics
Chitosan
Composite beads
Immobilization
Stability
Stability
Activated clay
Immobilization
Catalytic kinetics
Composite beads
Chitosan
Acid phosphatase
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Summary: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.
ISSN:1359-5113
1873-3298
DOI:10.1016/S0032-9592(03)00221-8