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Please use this identifier to cite or link to this item: http://repository.iitr.ac.in/handle/123456789/13325
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dc.contributor.authorKumar L.-
dc.contributor.authorDutt, Dharm-
dc.contributor.authorTapas S.-
dc.contributor.authorKumar, Pravindra R.Manish-
dc.date.accessioned2020-10-15T12:31:36Z-
dc.date.available2020-10-15T12:31:36Z-
dc.date.issued2013-
dc.identifier.citationBiocatalysis and Agricultural Biotechnology (2013), 2(3): 267-277-
dc.identifier.issn18788181-
dc.identifier.urihttps://doi.org/10.1016/j.bcab.2013.04.004-
dc.identifier.urihttp://repository.iitr.ac.in/handle/123456789/13325-
dc.description.abstractPresent study aims at purifying and characterizing crude xylanase isolated from Coprinus cinereus LK-D-NCIM-1369 under solid-state fermentation conditions. Crude xylanase is purified by (NH4)2SO4 precipitation, carboxymethyl cellulose cation-exchange and gel filtration chromatography with Superdex-200 column. Purified xylanase from C. cinereus shows 54.3% similarity with β-1,4 endoxylanase from C. cinerea okayama7#130 with accession number gi|169855830 based on MALDI-TOF/TOF. The purified xylanase-a monomeric protein with molecular weight 20.1kD shows maximum activity at 60°C and pH 7.0 and stable over pH 5.0-9.0 and temperature up to 70°C. The xylanase shows Km and V values of 3.26mg/mL and 909.09μm/min/mg for birchwood xylan. A sequence of 186 amino acids of C. cinerea okayama7#130 gi|169855830 is retrieved from NCBI database and its 3-D model is generated on the basis of crystal structure of xylanase 1XNK-A from Chaetomium thermophilum with the help of online server SWISS-MODEL workspace. The model is verified and validated on SAVES and PROCHECK programmes, respectively. Ramachandran plot reveals that the total residues in allowed and generously allowed regions are 99.4% and 0.6% respectively. Overlapping of xylanase with the template of 1XNK-A stipulates the amino acid residues Asn35, Tyr68, Arg113, Ser118, Tyr168 and Glu174 constitute active site of the enzyme. © 2013 Elsevier Ltd.-
dc.language.isoen_US-
dc.relation.ispartofBiocatalysis and Agricultural Biotechnology-
dc.subjectDocking-
dc.subjectHomology modeling-
dc.subjectMALDI-TOF/TOF-
dc.subjectPurification-
dc.subjectThermo-pH-stability-
dc.subjectXylanase-
dc.titlePurification, bio-chemical characterization, homology modeling and active site binding mode interactions of thermo-alkali-tolerant β-1,4 endoxylanase from Coprinus cinereus LK-D-NCIM-1369-
dc.typeArticle-
dc.scopusid57208572291-
dc.scopusid7005982560-
dc.scopusid35491918300-
dc.scopusid55064809000-
dc.affiliationKumar, L., Department of Paper Technology, Indian Institute of Technology Roorkee, Saharanpur Campus, Saharanpur 247001, India-
dc.affiliationDutt, D., Department of Paper Technology, Indian Institute of Technology Roorkee, Saharanpur Campus, Saharanpur 247001, India-
dc.affiliationTapas, S., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee 247667, India-
dc.affiliationKumar, P., Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee 247667, India-
dc.description.fundingThe first author is thankful to the Council of Scientific and Industrial Research , New Delhi for awarding him Senior Research Fellowship and for providing partial financial support to carry out this work.-
dc.description.correspondingauthorDutt, D.; Department of Paper Technology, Indian Institute of Technology Roorkee, Saharanpur Campus, Saharanpur 247001, India; email: dharmduttiit@gmail.com-
Appears in Collections:Journal Publications [PT]

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