Purified endoglucanase from C. biazotea mutant 51SMr was successfully immobilized on Eudragit L-100, with 75 % yield of immobilization. This method improved the kinetic and thermodynamic properties of the enzyme. Immobilization significantly decreased entropy and enthalpy of inactivation of biocatalyst and made it functionally and thermodynamically more stable and reusable compared to free one.
Keywords: Eudragit L-100, immobilization kinetics, melting point, substrate binding energy, thermodynamics, transition state stabilization
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