Immobilization of Chymotrypsin on the Microcapsule Surface and Enzymatic Activity of the Immobilized Chymotrypsin

Polyamide microcapsules with many carboxyl groups in their membranes were prepared using an interfacial polymerization technique, and α-chymotrypsin was covalently immobilized to their surface. The enzymatic activity of the immobilized α-chymotrypsin was measured and compared with that of intact α-c...

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Bibliographic Details
Published in:KOBUNSHI RONBUNSHU 1986/10/25, Vol.43(10), pp.665-668
Main Authors: SUMIDA, Shuji, MURAMATSU, Nobuhiro, KONDO, Tamotsu
Format: Article
Language:eng ; jpn
Subjects:
Enzymatic Activity
Enzyme Immobilization
Microcapsule Membrane
α-Chymotrypsin
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Summary:Polyamide microcapsules with many carboxyl groups in their membranes were prepared using an interfacial polymerization technique, and α-chymotrypsin was covalently immobilized to their surface. The enzymatic activity of the immobilized α-chymotrypsin was measured and compared with that of intact α-chymotrypsin in solution. Michaelis constant for α-chymotrypsin at the optimum pH for enzymatic activity was found to change inappreciably by immobilization while the maximum reaction velocity showed a considerable reduction after immobilization. Due to the negative charges of the dissociated surface carboxyl groups, a slight shift of optimum pH for the enzymatic activity of the enzyme to the alkaline side was observed.
ISSN:0386-2186
1881-5685
DOI:10.1295/koron.43.665