Kinetics of alpha-chymotrypsin catalyzed hydrolysis of 4-nitrophenyl acetate in ethanolamine surfactants.
The kinetics of alpha-chymotrypsin (alpha-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-Mcnten kinetics, the catalytic rate constant kcat and the Michaelis constant KM have been determined. The bell-shaped profiles of alpha-CT activity with increasing surfactant concentrations indicate the interaction between the micelle-bound enzyme and substrate.
Ghosh
Kallol K
KK
School of Studies in Chemistry, Pt. Ravishankar Shukla University, Raipur (C.G.), 492010, India. kallolkghosh@yahoo.com
Verma
Santosh Kumar
SK
D055162:Biocatalysis; D002918:Chymotrypsin / Q000378:metabolism*; D019856:Ethanolamine / Q000737:chemistry*; D006868:Hydrolysis; D007700:Kinetics; D009596:Nitrophenols / Q000378:metabolism*; D013501:Surface-Active Agents / Q000737:chemistry*
D009596:Nitrophenols; D013501:Surface-Active Agents; D019856:Ethanolamine; C008642:4-nitrophenyl acetate; D002918:Chymotrypsin; C117608:alpha-chymotrypsin