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

Yan Hong Ran; Zhi Fei Che; Wan Qun Chen

doi:10.4028/www.scientific.net/AMM.138-139.1067

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HomeApplied Mechanics and MaterialsApplied Mechanics and Materials Vols. 138-139Co-Immobilized Lignin Peroxidase and Manganese...

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.

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Periodical:

Applied Mechanics and Materials (Volumes 138-139)

Pages:

1067-1071

DOI:

https://doi.org/10.4028/www.scientific.net/AMM.138-139.1067

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Online since:

November 2011

Authors:

Yan Hong Ran, Zhi Fei Che, Wan Qun Chen

Keywords:

Chitosan Microsphere, Co-Immobilization, Lignin Peroxidase, Manganese Peroxidase

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References

[1] Y. Satyawali, M. Balakrishnan. Wastewater treatment in molasses-based alcohol distilleries for COD and color removal: A review. Journal of Environmental Management 2008: 86: 481–497.

DOI: 10.1016/j.jenvman.2006.12.024

Google Scholar

[2] Moreira MT, et al. . Manganese peroxidase production by Bjerkandera sp BOS55. Bioproc Eng, 2000, 23: 657–61.

DOI: 10.1007/s004490000216

Google Scholar

[3] Tekere M, et al,. Growth, dye degradation, and ligninolytic activity studies on Zimbabwean white-rot fungi. Enz Microb Technol . 2001, 28: 420–6.

DOI: 10.1016/s0141-0229(00)00343-4

Google Scholar

[4] Yaropolov AI, et al, Laccase: properties, catalytic mechanism and applicability. Appl Biochem Biotech. 1994, 49: 257– 80.

Google Scholar

[5] Giardina P, et al,. Cloning and sequencing of a laccase gene from Pleurotus ostreatus. Appl Environ Microbiol , 1995, 61: 2408 –13.

DOI: 10.1128/aem.61.6.2408-2413.1995

Google Scholar

[6] Eggert C, et al. The ligninolytic system of the white rot fungus Pycnoporus cinnabarinus: purification and characterization of the laccase. Appl Environ Microbiol, 1996; 62: 1151– 8.

DOI: 10.1128/aem.62.4.1151-1158.1996

Google Scholar

[7] P. Erbacher, S. Zou, et al. Chitosan based vector/DNA complexes for gene delivery: biophysical characteristics and transfection ability, Pharm. Res., 1998, 15 1332–1339.

Google Scholar

[8] K.W. Leong. DNA-polycation nanospheres as non-viral gene delivery vehicles, J. Cont. Rel, 1998, 53: 183–193.

DOI: 10.1016/s0168-3659(97)00252-6

Google Scholar

[9] T. Ishii, et al,. Mechanism of cell transfection with plasmid/chitosan complex, Biochim. Biophys. , 2001, 51: 51–64.

Google Scholar

[10] Xiaolin l., et al. Simultaneous isolation and immobilization of streptavidin-β-galactosidase: some kinetic characteristics of the immobilized enzyme and regeneration of bioreactors. Enzyme and Microbial Technology. 1996, 19: 378-383.

DOI: 10.1016/s0141-0229(96)00015-4

Google Scholar

[11] I. Mielgo, et al,. Covalent immobilization of manganese peroxidase (MnP) from phanerochaete chrysosporium and Bijerkandera sp. BOS55. Enzyme and Microbial Technology. 2003, 32: 769-775.

DOI: 10.1016/s0141-0229(03)00066-8

Google Scholar

[12] Ran Yanhong, YU Shujuan, Yang Liansheng et al. Decolorization of Refinery Effulent and Polysaccarrides Preparation by Polystictus Versicolor (In Chinese). Journal of South China University of Technology, Vol (31), 3, 200.

Google Scholar