Please use this identifier to cite or link to this item: http://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4500
Full metadata record
DC FieldValueLanguage
dc.contributor.authorHalaburgi V.M
dc.contributor.authorSharma S
dc.contributor.authorSinha M
dc.contributor.authorSingh T.P
dc.contributor.authorKaregoudar T.B.
dc.date.accessioned2020-06-12T15:04:06Z-
dc.date.available2020-06-12T15:04:06Z-
dc.date.issued2011
dc.identifier.citationProcess Biochemistry , Vol. 46 , 5 , p. 1146 - 1152en_US
dc.identifier.uri10.1016/j.procbio.2011.02.002
dc.identifier.urihttp://gukir.inflibnet.ac.in:8080/jspui/handle/123456789/4500-
dc.description.abstractThe fungus Cladosporium cladosporioides was isolated from a coal sample as a dye decolorizing microorganism. The maximum production of laccase from this fungus was found to be 4160 U/l with 0.05 mM CuSO4, 4% (w/v) glucose and lignin 0.04% (w/v). The laccase was purified from C. cladosporioides to homogeneity in a very active state using ammonium salt precipitation and gel permeation chromatography. Analysis with SDS-PAGE showed that the purified laccase was a monomeric protein of 71.2 kDa, and the apparent molecular mass of this enzyme was 75.17 kDa (m/z = 75,174), which was accurately determined by MALDI/TOF-MS. The UV-vis absorbance and electron paramagnetic resonance spectra of the purified laccase showed the presence of type 1 and type 3 copper ions. The optimum pH and temperature of the purified laccase were 3.5 and 40-70 °C, respectively, and the N-terminal amino acid sequence was determined to be IGPTGDMYIVNEDVS. The purified laccase was effective in the biotransformation of aromatic compounds as well as in the decolorization of various dyes. © 2011 Elsevier Ltd. All rights reserved.en_US
dc.subjectBiotransformation
dc.subjectCladosporium cladosporioides
dc.subjectDecolorization
dc.subjectLaccase
dc.subjectN-terminal amino acid sequence
dc.titlePurification and characterization of a thermostable laccase from the ascomycetes Cladosporium cladosporioides and its applicationsen_US
dc.typeArticle
Appears in Collections:1. Journal Articles

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.