Co-immobilized Lignin Peroxidase and Manganese Peroxidase From Coriolus Versicolor Capable of Decolorizing Molasses Waste Water

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 degrees 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 degrees 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.