Co-Immobilized Lignin Peroxidase and Manganese Peroxidase from Coriolus Versicolor Capable of Decolorizing Molasses Waste Water

Abstract

This paper explains how the Lignin peroxidase and Manganese Peroxidase from Coriolus Versicolor were co-immobilized by chitosan microspheres.It studies kinetic character of the enzyme after co-immobilization.Optimum Lip and MnP activity obtained at 30-35°C for 14 hours in pH 8.4 glutaraldehyde solutions during immobilized to chitosan microspheres which prepared by coagulation in NaOH: methanol=3:2. When kept at 50°C for 6h, more than 80% of the immobilized enzyme activity remained, while the free enzymes were inactive under the same conditions. The co-immobilized enzyme can remain 70% activity after two weeks while both of the free enzymes inactive. Compared with the free enzymes, temperature and time stability of the co-immobilized enzyme was considerably improved.