Effects of ionic surfactants used in reversed micelles on cutinase activity and stability.

The effects of aqueous surfactant solutions on the kinetics and stability of cutinase from Fusarium solani pisi were studied. The surfactant sodium bis[2-ethylhexyl]ester sulfosuccinic acid (AOT) acts as a pseudo-competitive inhibitor within a limited concentration range relative to the hydrolysis of short-chain p-nitrophenyl esters. For higher concentrations a hyperbolic mixed inhibition takes place. A pseudo-activation of hydrolysis in presence of AOT and hexadecyltrimethyl-ammonium bromide (CTAB) was observed. CTAB has similar effects on kinetics of cutinase. Cutinase revealed to be stable in CTAB solutions, with activity retention as high as 80%. AOT has a deleterious effect on the enzyme in the time course, resulting in acute loss of activity possibly related with unfolding of the protein structure. A relation between deactivation rate constants and AOT/cutinase concentration ratios is suggested. The presence of the linear alcohol, 1-hexanol, was included in these solutions, in the attempt to interpret the deactivation of cutinase when encapsulated in reversed micelle systems in the absence of this co-surfactant.