[Effect of soluble matrix on the stability of modified alpha-chymotrypsin].

alpha-Chymotrypsin preparations covalently bound by Shiff bases with water soluble oxidated dextran and alginate are obtained to study the effect of charged and neutral matrices on the enzymes stability under their modification by polymers. Water soluble enzyme preparations show a catalytic activity and have a slightly enhanced thermostability. Thermostability of alpha-chymotrypsin modified by a negatively charged polymer is increased owing to the reducing of activation entropy of the denaturation reaction, while the increase of the stability of neutral polymer (dextran) modified enzyme is due to the increase of activation enthalpy of the denaturation reaction.