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°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.
Y. H. Ran et al., "Co-Immobilized Lignin Peroxidase and Manganese Peroxidase from Coriolus Versicolor Capable of Decolorizing Molasses Waste Water", Applied Mechanics and Materials, Vols. 138-139, pp. 1067-1071, 2012