Immobilization and Reusability Efficiency of Laccase Onto Different Matrices Using Different Approaches

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Laccase has been recognized as lignocellulose oxidase enzyme which is involved in bioremediation, chemical synthesis, bio-bleaching of paper pulp, bio-sensing, textile finishing and wine stabilization. The immobilization of enzymes offers several advantages for enzyme based catalysis because the storage and operational stabilities of enzymes are frequently enhanced. Including this, the reusability of immobilized enzymes exhibits a key advantage with respect to free enzymes. In this study various immobilization approaches were employed with different polymers, inorganic materials and glass beads. It was observed that the enzyme immobilized to glass beads exhibited the highest residual activity of 92% which was followed by the polypropylene (86%). Including this, the efficiency of reusability of immobilized laccase was also evaluated up to 10 successive cycles, and it was observed that the efficiency of immobilized enzyme was reduced from 1st cycle to 10th cycle.