The immobilization of laccase enzyme from Trametes versicolor on the surface of porous zinc oxide nanoparticles and studying features of the immobilized enzyme
Subject Areas : International Journal of Bio-Inorganic Hybrid Nanomaterials
Keywords: Immobilization, Laccase, Porous ZnO nanoparticles, Stability, Reusability, Tramitis versicolor,
Abstract :
The laccase enzyme is the largest group of Oxidoreductase enzymes and is capable ofoxidizing a wide range of organic substrates to water along with molecular oxygen resuscitation. ZnOnanoparticles are known for their specific properties such as chemical stability, high electrochemicalcoupling rates, and wide range of absorption of radiation as multifunctional compounds. In this study,ZnO porous nanoparticles were synthesized and then the laccase enzyme was stabilized from the sourceof vermicellum tramitis by surface absorption method on the surface of synthesized nanoparticles. Inthe following, kinetic parameters, temperature stability, reusability and sustainability of the stabilizedenzyme were measured and compared with the free enzyme. Given the results obtained at all threetemperatures (40, 50 and 60 °C), the stabilized enzyme shows more temperature stability than the freeenzyme in desired time range. The kinetic parameters Vm and Km did not significantly change withrespect to the free enzyme. Enzyme activity returned to zero after 10 cycles of use and recycling. Whilethe free enzyme lost its activity after three weeks of maintenance in laboratory condition, the stabilizedenzyme retained 30% of its initial activity. These results indicate that ZnO porous nanoparticles can beused as a suitable substrate for the stabilization of laccase enzyme by surface adsorption method, andimproves the stability parameters of the enzyme without affecting the kinetic properties of the enzyme.