Activity of carboxypeptidase A bound to a modified cellulosic matrix

Carboxypeptidase A immobilized on acid chloride of oxidized cellulose showed the following features: (a) as indicated by the linearity of reaction kinetics, the immobilized enzyme action is not diffusion controlled; (b) greater flow rates are achievable with less clogging during continual usage sinc...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 1986-01, Vol.12 (2), p.107-119
Main Authors: SANJAY KUMAR, PADMA VASUDEVAN, DUA, R. D
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Biotechnology
carboxypeptidase A
cellulose
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Immobilization of enzymes and other molecules
Immobilization techniques
immobilized enzymes
Methods. Procedures. Technologies
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Summary:Carboxypeptidase A immobilized on acid chloride of oxidized cellulose showed the following features: (a) as indicated by the linearity of reaction kinetics, the immobilized enzyme action is not diffusion controlled; (b) greater flow rates are achievable with less clogging during continual usage since the enzyme is attached to a porous screen; (c) ease of handling; and (d) no apparent electrostatic interaction with the support material that is uncharged. The immobilized enzyme retained 60% of the original activity. The half-life of free enzyme was only 20 min, whereas for immobilized enzyme it was enhanced up to 2 h 48 min. It could be recovered and repeatedly used.
ISSN:0273-2289
1559-0291