Kinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants
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Title |
Kinetics of α-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants
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Creator |
Ghosh, Kallol K
Verma, Santosh Kumar |
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Subject |
α-Chymotrypsin
4-Nitrophenyl acetate Hydrolysis Micellar enzymology Alkyldimethyl ethanolammonium bromide Surfactants |
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Description |
350-353
The kinetics of α-chymotrypsin (α-CT) catalyzed hydrolysis of 4-nitrophenyl acetate has been studied in aqueous solution of alkyldimethylethanolammonium bromide (cetyl, dodecyl, decyl) surfactants at concentrations below and above their critical micelle concentration. From Michaelis-Menten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The bell-shaped profiles of α-CT activity with increasing surfactant concentrations indicate the interaction between the micelle-bound enzyme and substrate. |
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Date |
2008-11-06T04:14:55Z
2008-11-06T04:14:55Z 2008-10 |
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Type |
Article
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Identifier |
0301-1208
http://hdl.handle.net/123456789/2378 |
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Language |
en_US
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Publisher |
CSIR
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Source |
IJBB Vol.45(5) [October 2008]
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