Betty Meuwiah Faulet1 , SÃ©bastien NiamkÃ©2,*, Jean Tia Gonnety1 and Lucien Patrice KouamÃ©
A xylanase was purified from symbotic fungus, Termitomyces sp. by chromatography on columns of DEAE-Sepharose, CM-Sepharose, gel filtration and Phenyl-Sepharose. The preparation was shown to be homogenous by polyacrylamide gel electrophoresis. The purified enzyme displayed two protein bands on SDS-polyacrylamide gel electrophoresis and its molecular mass was estimated to 80-87 kDa. The xylanase exhibited maximum activity at 65-70°C and at pH 5.6, but it retained more than 80% of its activity in the pH range 5.0-6.0. The enzyme was stable for a long time-period up to 50°C and for 1 h at 60°C. Although the xylanase had a lower carboxymethylcellulase activity, it lacked activity towards substituted xylan, xylobiose, inulin, starch, polygalacturonic acid or pNP-glycosides. Kinetic parameters indicated higher efficiency in the hydrolysis of beechwood xylan and birchwood xylan. The xylanase activity was stimulated by K+ , Mn2+ and dithiol-reducing agents and was sensitive to Cu2+ , Fe2+, Zn2+ and detergent agents. The enzymatic activity was observed in presence of urea up to a 1% (w/v) concentration. The enzyme could also be used in the presence of organic solvents such as acetone or dioxane (5%, v/v) without loss of activity.
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