A surface immobilization method of endoglucanase from Cellulomonas biazotea mutant improved catalytic properties of biocatalyst during processing.
Purified endoglucanase from C. biazotea mutant 51SM(r) 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.
Rajoka
Muhammad Ibrahim
MI
Industrial Biotechnology Division, National Institute for Biotechnology and Genetic Engineering, Jhang Road, Faisalabad, Pakistan. mirajoka@nibge.org
Zia
Yasmin
Y
D002384:Catalysis; D002480:Cellulase / Q000378:metabolism*; D040143:Cellulomonas / Q000201:enzymology* / Q000235:genetics; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D009154:Mutation; D013379:Substrate Specificity; D013816:Thermodynamics
D004800:Enzymes, Immobilized; D002480:Cellulase