Please use this identifier to cite or link to this item: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8959
Title: Multicopper oxidase (MCO) laccase from Stropharia sp. ITCC‑8422: an apparent authentication using integrated experimental and in silico analysis
Authors: Agrawal, Komal
Shankar, Jata
Verma, Pradeep
Keywords: Laccase
Docking
In silico
Alizarin cyanine green
Bioremediation
Issue Date: 2020
Publisher: Jaypee University of Information Technology, Solan, H.P.
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 agreement.
URI: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/8959
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