Effect of the polymer matrix on the thermal stability of immobilized trypsin

Abstract

Trypsin was immobilized by radiation polymerization of various monomers at low temperatures, and the effects of the polymer matrix on the enzyme activity and thermal stability were studied. The shape and structure of the polymer matrix for the immobilized enzymes changed on changing the nature of the monomers. Enzyme activity and thermal stability were affected by the molecular structure and concentration of monomers. The maximum thermal stability of the immobilized enzymes was achieved with a degree of polymer hydration of about 0.5, but the thermal stability decreased at lower and higher degrees of hydration.