Effects of Head Group of Cationic Surfactants on the Hydrolysis of p-Nitrophenyl Acetate Catalyzed by α-Chymotrypsin

被引:20
作者
Ghosh, Kallol K. [1 ]
Verma, Santosh Kumar [1 ]
机构
[1] Pt Ravishankar Shukla Univ, Sch Studies Chem, Raipur 492010, Madhya Pradesh, India
关键词
LIPASE ACTIVITY PROFILE; AQUEOUS-SOLUTIONS; 2-NAPHTHYL ACETATE; INTERFACIAL BINDING; REVERSE MICELLES; KINETICS; SUPERACTIVITY; HEADGROUP; MICROEMULSIONS; AGGREGATION;
D O I
10.1002/kin.20408
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 kinetics of hydrolysis of p-nitrophenyl acetate catalyzed by alpha-chymotrypsin (alpha-CT) has been studied in the presence of several cationic surfactants having different head groups maintaining the dodecyl hydrophobic residue and bromide counterion. The enzyme activity was tested in the presence of dodecyl trimethylammonium bromide (DTAB), dode-cylpyridinium bromide (DPB), dodecyldimethylethanolammonium bromide (DDMEAB), dodecyldiethylethanolammonium bromide (DDEEAB), benzyldimethyldodecylammonium bromide (BDDAB), and dodecyltriphenylphosphonium bromide (DTPB) surfactants. The extent of superactivity depends upon head groups of surfactants. The activity of alpha-CT depends on the surfactant concentration and it varies with the surfactant head group dimensions (DTPB > DDEEAB > DTAB > BDDAB > DDMEAB > DPB). For all surfactants, DTPB exhibits highest superactivity. The effects of surfactants on the apparent kinetic parameters like Michaelis constant K-m and the catalytic constant k(cat) have been determined. (C) 2009 Wiley Periodicals, Inc. Int J Chem Kinet 41: 377-381, 2009
引用
收藏
页码:377 / 381
页数:5
相关论文
共 33 条
[1]   Kinetics of N-glutaryl-L-phenylalanine p-nitroanilide hydrolysis catalyzed by α-chymotrypsin in aqueous solutions of dodecyltrimethylammonium bromide [J].
Abuin, E ;
Lissi, E ;
Duarte, R .
JOURNAL OF COLLOID AND INTERFACE SCIENCE, 2005, 283 (02) :539-543
[2]   Distinct effect of a cationic surfactant on the transient and steady state phases of 2-naphthyl acetate hydrolysis catalyzed by α-chymotrypsin [J].
Abuin, E ;
Lissi, E ;
Duarte, R .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2004, 31 (4-6) :83-85
[3]   Kinetics of 2-naphthyl acetate hydrolysis catalyzed by α-chymotrypsin in aqueous solutions of dodecyltrimethylammonium bromide [J].
Abuin, E ;
Lissi, E ;
Duarte, R .
LANGMUIR, 2003, 19 (13) :5374-5377
[4]   Kinetics of p-nitrophenyl acetate hydrolysis catalyzed by Mucor java']javanicus lipase in AOT reverse micellar solutions formulated in different organic solvents [J].
Abuin, Elsa ;
Lissi, Eduardo ;
Biasutti, M. Alicia ;
Duarte, Roxanna .
PROTEIN JOURNAL, 2007, 26 (07) :475-479
[5]   Kinetics of N-glutaryl-L-phenylalanine p-nitroanilide hydrolysis catalyzed by α-chymotrypsin in aqueous solutions of alkyltrimethylammonium bromides [J].
Abuin, Elsa ;
Lissi, Eduardo ;
Calderon, Cristian .
JOURNAL OF COLLOID AND INTERFACE SCIENCE, 2007, 308 (02) :573-576
[6]   α-chymotrypsin superactivity in cetyltrialkylammonium bromide-rich media [J].
Alfani, F ;
Cantarella, M ;
Spreti, N ;
Germani, R ;
Savelli, G .
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2000, 88 (1-3) :1-15
[7]  
ANGELIS FD, 2003, ORG BIOCH, V268, P3125
[8]   Kinetics of reactions catalyzed by enzymes in solutions of surfactants [J].
Biasutti, Maria A. ;
Abuin, Elsa B. ;
Silber, Juana J. ;
Correa, N. Mariano ;
Lissi, Eduardo A. .
ADVANCES IN COLLOID AND INTERFACE SCIENCE, 2008, 136 (1-2) :1-24
[9]   Caging enzyme function:: α-chymotrypsin in reverse micelle [J].
Biswas, R ;
Pal, SK .
CHEMICAL PHYSICS LETTERS, 2004, 387 (4-6) :221-226
[10]   Superactivity and conformational changes on α-chymotrypsin upon interfacial binding to cationic micelles [J].
Celej, MS ;
D'Andrea, MG ;
Campana, PT ;
Fidelio, GD ;
Bianconi, ML .
BIOCHEMICAL JOURNAL, 2004, 378 :1059-1066