Purification and Characterization of the Xylanase Produced by Jonesia denitrificans BN-13 |
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Authors: | Nawel Boucherba Mohammed Gagaoua Estelle Copinet Azeddine Bettache Francis Duchiron Said Benallaoua |
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Affiliation: | 1. Laboratory of Applied Microbiology, Faculty of Nature Science and Life, University of Bejaia, Targa Ouzemmour, 06000, Bejaia, Algeria 3. INATAA, Bioqual Laboratory, Université de Constantine 1, Route de Ain El-Bey, 25000, Constantine, Algeria 2. UMR FARE 614 INRA/URCA, Laboratory of Industrial Microbiology, UFR Sciences, University of Reims Champagne-Ardenne, Moulin de la Housse, BP 1039, 51687, Reims, France
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Abstract: | Jonesia denitrificans BN-13 produces six xylanases: Xyl1, Xyl2, Xyl3, Xyl4, Xyl5, and Xyl6; the Xyl4 was purified and characterized after two consecutive purification steps using ultrafiltration and anion exchange chromatography. The xylanase-specific activity was found to be 77 unit (U)/mg. The molecular weight of the Xyl4 estimated using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) revealed a monomeric isoenzyme of about 42 kDa. It showed an optimum pH value of 7.0 and a temperature of 50 °C. It was stable at 50 °C for 9.34 h. The enzyme showed to be activated by Mn+2, β-mercaptoethanol, and dithiothreitol (DTT) with a high affinity towards birchwood xylan (with a K m of 1 mg ml?1) and hydrolysis of oat-spelt xylan with a K m of 1.85 mg ml?1. The ability of binding to cellulose and/or xylan was also investigated. |
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