High‐pressure stabilization of α‐chymotrypsin entrapped in reversed micelles of aerosol OT in octane against thermal inactivation

FEBS Letters

Saldana, J.-L.²  Balny, Claude²  Mozhaev, Vadim V.¹  Bec, Nicole²  Klyachko, Natalia L.¹  Rariy, Roman V.¹  Levashov, Andrey V.¹  Nametkin, Sergey N.¹ 

[1] Division of Chemical Enzymology, Department of Chemistry, Moscow State University, 000958 Moscow, Russian Federation;INSERM U 128, BP 5051 (CNRS), 34033 Montpellier Cedex 1, France

关键词: Thermal inactivation of enzyme;    Stabilization of enzyme;    Regulation of enzyme activity;    High pressure;    Micellar enzymology;    Baroenzymology;    CT;    α-chymotrypsin;    spdium bis-(2-ethylhexyl)-sulfosuccinate;    AOT;    Aerosol OT;    SPNA;    p-nitroanilide;    w 0 = [H2O]/[AOT];    i.e. w 0 is equal to the ratio between the concentrations of water and surfactant in a micellar system;   

DOI  :  10.1016/0014-5793(95)00344-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Chymotrypsin (CT) solubilized in reversed micelles of sodium bis-(2-ethylhexyl)-sulfosuccinate (AOT) undergoes thermal inactivation and the enzyme stability decreases significantly when temperature increases (25–40°C). The half-life of CT in micelles shows a bell-shaped dependence on the degree of hydration of AOT (w ₀) analogous to the previously obtained dependence on w ₀ for the enzyme activity. The optima of catalytic activity and thermal stability have been observed under conditions where the diameter of the inner aqueous cavity of the micelle is close to the size of the enzyme molecule (w ₀ = 10). Application of high hydrostatic pressure in the range of 1–1500 atm (bar) stabilizes CT against thermal inactivation at all hydration degrees (w ₀) from 7 to 20; the stabilization effect is most pronounced under the experimental conditions being far from the optimum for catalytic activity.

【 授权许可】

Unknown