Nonionic tensides modify papain structure and proteolytic activity

The effect of 33 polyethoxylated nonionic tensides with various hydrophobic moieties was studied on the proteolytic activity and phase transition behaviour of papain. Tensides with longer ethyleneoxide chain markedly increased the phase transition temperatures of papain indicating possible hydrogen bond formation between the hydrophilic ethyleneoxide chain and the polar substructures of papain. The character of lipophilic moiety of tensides influences also each physicochemical parameter of papain suggesting the existence of hydrophobic interactions too. The significant positive linear correlations between the activity increasing and structure stabilizing effects of tensides make probably that the structure modification of papain accounts for its enchanced proteolytic activity.