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Purification and kinetics study of thermostable cellulase free Xylanase from Bacillus subtilis

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Present study dealt with the production, purification and characterization of xylanase from Bacillus subtilis- BS05 grown in submerged fermentation at 37°C for 48h using sugarcane bagasse as a substrate. Xylanase enzyme was purified to homogeneity by ammonium sulphate fractionation followed by sephadex G-100 chromatography. The molecular mass of xylanase enzyme was found to be 23kDa by SDS-PAGE. The optimum pH and temperature of xylanase enzyme was 5 and 50°C with stability range of 5-6 and 30°C -5°C respectively. The enzyme had half life of 1386-1155 minutes at 30°C -50°C respectively. Metal profile of the enzyme showed that Mn2+ (127.4 %) and Fe2+ (115%) were the activators while Hg2+ (14%) and EDTA (19%) were the inhibitors. Kinetic parameters revealed that the enzyme is specific to birchwood xylan with Km, Kcat, Vmax and Kcat/Km value of 1.15 mg/ml, 850 s-1, 117.64 U/mg and 739.13 s-1 mg-1.mL respectively.
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Keywords: Bacillus sp; Xylanase; characterization; purification

Document Type: Research Article

Publication date: November 1, 2013

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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