Influence of water-miscible aprotic solvents on alpha-chymotrypsin stability

被引：24
|
作者：
Lozano, P [1 ]
deDiego, T [1 ]
Iborra, JL [1 ]
机构：
[1] UNIV MURCIA, FAC QUIM, DEPT BIOQUIM & BIOL MOL & INMUNOL B, E-30001 MURCIA, SPAIN
来源：
BIOTECHNOLOGY PROGRESS | 1996年 / 12卷 / 04期
关键词：
D O I：
10.1021/bp960011p
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
The influence of five different water-miscible aprotic solvents (dimethyl sulfoxide, dimethylformamide, acetonitrile, acetone, and tetrahydrofuran) on the stability of immobilized alpha-chymotrypsin adsorbed onto Celite, has been studied. In all cases, alpha-chymotrypsin exhibited non-first-order deactivation kinetics, which were adequately analyzed by a two-step series-type deactivation model. The main effects of solvents were observed in the first-step of the kinetic mechanism. The most hydrophilic solvent (DMSO) enhanced greatly the enzyme stability, while the increase in solvent hydrophobicity determines a loss in their protective effect. For the most assayed hydrophobic solvent (THF) a denaturative effect was always showed. These facts were also observed from the analysis of the evolution of the half-live of the enzyme, as a function of the solvent concentrations and the water distribution between both the macro- and microenvironment of the enzyme.
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页码：488 / 493
页数：6
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