Effect of Cationic Surfactants on the Enzymatic Activity of α-Chymotrypsin

被引：11
|
作者：
Verma, S. K. [1 ]
Ghosh, K. K. [1 ]
机构：
[1] Pt Ravishankar Shukla Univ, Sch Studies Chem, Raipur 492010, CG, India
来源：
KINETICS AND CATALYSIS | 2011年 / 52卷 / 01期
关键词：
INTERFACIAL BINDING; AQUEOUS-SOLUTIONS; HYDROLYSIS; KINETICS; ACETATE; MECHANISM; MICELLES; DYNAMICS; LIPASE;
D O I：
10.1134/S0023158411010216
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
The hydrolysis of p-nitrophenyl benzoate catalyzed by alpha-chymotrypsin in the presence of cetyltriphenylphosphonium bromide, cetyltributylphosphonium bromide and cetyltrimethylammonium bromide (pre and post micellar regions) has been studied. The ester is hydrolyzed readily by alpha-chymotrypsin in all the surfactants with the highest activity shown in cetyltributylphosphonium bromide. The dependences of the Michaelis constant and the catalytic constant with surfactant concentration have also been discussed.
引用
收藏
页码：6 / 10
页数：5
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