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This work is licensed under a Creative Commons Attribution 4.0 International License.
Purification and Characterization of Laccase from Ceriporiopsis subvermispora
Corresponding Author(s) : Hong Xu
Asian Journal of Chemistry,
Vol. 26 No. 15 (2014): Vol 26 Issue 15
Abstract
Laccase from Ceriporiopsis subvermispora was purified and partially characterized using a combination of ammonium sulfate precipitation, DEAE-cellulose ion exchange chromatography and Sephadex G-100 molecular sieve column chromatography. The results demonstrated that the maximum laccase output from C. subvermispora fermentation reached 3900 U/L. The specific activity of the laccase increased from 10.28 U/mg in a crude enzyme solution to 245.27 U/mg after isolation and purification, with a purification factor of 23.86 and a yield of 24.40 %. The molecular mass of laccase was 63 kDa and the Michaelis-Menten constant value was 23.3 μmol/L. The optimal temperature for enzyme activity was 50 °C. The stabilization pH range was 4-5; within a pH 4-5 range, the relative activity was higher than 70 %.
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H. Bermek, K. Li and K.L. Eriksson, Bioresour. Technol., 85, 249 (2002); doi:10.1016/S0960-8524(02)00132-3.
C.E. Wyman, B.E. Dale, R.T. Elander, M. Holtzapple, M.R. Ladisch and Y.Y. Lee, Bioresour. Technol., 96, 1959 (2005); doi:10.1016/j.biortech.2005.01.010.
D.S. Arora and P.K. Gill, Bioresour. Technol., 77, 89 (2001); doi:10.1016/S0960-8524(00)00114-0.
M. Fenice, G. Giovannozzisermanni, F. Federici and A. Dannibale, J. Biotechnol., 100, 77 (2003); doi:10.1016/S0168-1656(02)00241-9.
P. Baborová, M. Möder, P. Baldrian, K. Cajthamlová and T. Cajthaml, Res. Microbiol., 157, 248 (2006); doi:10.1016/j.resmic.2005.09.001.
K. Fackler, C. Gradinger, B. Hinterstoisser, K. Messner and M. Schwanninger, Enzyme Microb. Technol., 39, 1476 (2006); doi:10.1016/j.enzmictec.2006.03.043.
K. Murugesan, I.-H. Nam, Y.-M. Kim and Y.-S. Chang, Microb. Technol., 40, 1662 (2007); doi:10.1016/j.enzmictec.2006.08.028.
E. Abadulla, T. Tzanov, S. Costa, K.-H. Robra, A. Cavaco-Paulo and G.M. Gubitz, Appl. Environ. Microbiol., 66, 3357 (2000); doi:10.1128/AEM.66.8.3357-3362.2000.
G. Songulashvili, V. Elisashvili, S.P. Wasser, E. Nevo and Y. Hadar, Enzyme Microb. Technol., 41, 57 (2007); doi:10.1016/j.enzmictec.2006.11.024.
K.M. Park and S.S. Park, J. Microbiol. Biotechnol., 18, 670 (2008).
S. Vikineswary, N. Abdullah, M. Renuvathani, M. Sekaran, A. Pandey and E. Jones, Bioresour. Technol., 97, 171 (2006); doi:10.1016/j.biortech.2005.02.015.
D. Litthauer, M.J. van Vuuren, A. van Tonder and F.W. Wolfaardt, Enzyme Microb. Technol., 40, 563 (2007); doi:10.1016/j.enzmictec.2006.05.011.
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A. Ferraz, A.M. Cordova and A. Machuca, Enzyme Microb. Technol., 32, 59 (2003); doi:10.1016/S0141-0229(02)00267-3.
K. Yaghoubi, M. Pazouki and S.A. Shojaosadati, Bioresour. Technol., 99, 4321 (2008); doi:10.1016/j.biortech.2007.08.043.
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V. Elisashvili and E. Kachlishvili, J. Biotechnol., 144, 37 (2009); doi:10.1016/j.jbiotec.2009.06.020.