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

Bioprocess Biosyst Eng. 2021 Nov;44(11):2417-2427. doi: 10.1007/s00449-021-02614-7. Epub 2021 Jul 18.

Abstract

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-1, respectively. Irreversible inactivation energy of free and immobilized CMCase was 96.43 and 99.01 kJ mol-1, respectively. Similarly, the enthalpy of deactivation (ΔHd) values for free and immobilized enzyme were found to be in the range of 93.51-93.76 kJ mol-1 and 96.08-96.33 kJ mol-1, respectively. Michaelis-Menten constant (Km) increased from 1.267 ± 0.06 to 1.5891 ± 0.07 mg ml-1 and the maximum reaction rate (Vmax) value decreased (8319.47 ± 416 to 5643.34 ± 282 U ml-1 min-1) 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.

Keywords: Carboxymethyl cellulose; Cellulose; Immobilization; Kinetics; Thermodynamics.

MeSH terms

  • Acrylic Resins / chemistry*
  • Catalysis
  • Cellulase / metabolism*
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism
  • Kinetics
  • Temperature
  • Thermodynamics*

Substances

  • Acrylic Resins
  • Enzymes, Immobilized
  • polyacrylamide
  • Cellulase
  • carboxymethylcellulase