Please use this identifier to cite or link to this item: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8340
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dc.contributor.authorAgrawal, Komal-
dc.contributor.authorShankar, Jata-
dc.contributor.authorVerma, Pradeep-
dc.date.accessioned2022-11-23T09:09:05Z-
dc.date.available2022-11-23T09:09:05Z-
dc.date.issued2020-
dc.identifier.urihttp://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8340-
dc.description.abstract(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), 2,6-dimethoxyphenol (DMP), guaiacol (GCL) and syringaldazine (SYZ) was determined. It exhibited maximum affinity against ABTS, followed by DMP and negligible activity for GCL and SYZ. As the concentration of substrate increased from 0.5 to 1.5 mM (ABTS) and 1 to 5 mM (DMP), the activity increased from 301.1 to 567.8 U/L and 254.4 to 436.2 U/L. Further, quadrupole time-of-flight liquid chromatography mass spectrometry (QTOF-LCMS) analysis of the extracellular proteome of Stropharia sp. ITCC-8422 identified eighty-four (84) extracellular proteins. The peptide sequence for the enzyme of interest exhibited sequence similarity with laccase-5 of Trametes pubescens. Using high molecular mass sequence of laccase-5, the protein structure of laccase was modelled and binding energy of laccase with four substrates, i.e. ABTS (− 5.65), DMP (− 4.65), GCL (− 4.66) and SYZ (− 5.5) was determined using autodock tool. The experimental and in silico analyses revealed maximum activity of laccase and lowest binding energy with ABTS. Besides, laccase was purified and it exhibited 2.1-fold purification with purification yield of 20.4% and had stability of 70% at pH 5–9 and 30–40 ℃. In addition, the bioremediation potential of laccase was explored by in silico analysis, where the binding energy of laccase with alizarin cyanine green was − 6.37 and both in silico work and experimental work were in agreementen_US
dc.language.isoenen_US
dc.publisherJaypee University of Information Technology, Solan, H.P.en_US
dc.subjectLaccaseen_US
dc.subjectDockingen_US
dc.subjectIn silicoen_US
dc.subjectBioremediationen_US
dc.titleMulticopper oxidase (MCO) laccase from Stropharia sp. ITCC‑8422: an apparent authentication using integrated experimental and in silico analysisen_US
dc.typeArticleen_US
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