Thermodynamics, kinetics and optimization of catalytic behavior of polyacrylamide-entrapped carboxymethyl cellulase (CMCase) for prospective industrial use.

In the current study, kinetic and thermodynamic parameters of free and polyacrylamide-immobilized CMCase were analyzed. The maximum immobilization yield of 34 ± 1.7% was achieved at 11% acrylamide. The enthalpy of activation (ΔH) of free and immobilized enzyme was found to be 13.61 and 0.29 kJ mol, respectively. Irreversible inactivation energy of free and immobilized CMCase was 96.43 and 99.01 kJ mol, respectively. Similarly, the enthalpy of deactivation (ΔH) values for free and immobilized enzyme were found to be in the range of 93.51-93.76 kJ mol and 96.08-96.33 kJ mol, respectively. Michaelis-Menten constant (K) increased from 1.267 ± 0.06 to 1.5891 ± 0.07 mg ml and the maximum reaction rate (V) value decreased (8319.47 ± 416 to 5643.34 ± 282 U ml min) after immobilization. Due to wide pH and temperature stability profile with sufficient reusing efficiency up to three successive cycles, the immobilized CMCase might be useful for various industrial processes.