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Purification and properties of two xylanases from macrotermes muelleri termitidae macrotermitinae and its symbiotic fungus termitomyces sp


Purification and properties of two xylanases from macrotermes muelleri termitidae macrotermitinae and its symbiotic fungus termitomyces sp



Insect Biochemistry 18(7): 709-716



Two xylanases had been purified, the first from termite Macrotermes muelleri workers (xylanase XT) and the second from its symbiotic fungus Termitomyces sp. (xylanase XF) through successive liquid chromatographic steps on hydroxyapatite, DEAE sepharose and Mono PTM. The enzyme preparations were homogeneous as judged by gel electrophoresis. A 400-fold increase in specific activity (from the crude extract) was obtained. The apparent molecular weight of both xylanases determined by SDS-PAGE was 28.5 kDa. Their optimum ws 5.2 and their Km value determined with CMC as substrate was 0.5 .times. 10-3%. The enzymatic specificity, the glycoprotein nature, the thermal stability of both enzymes and the effect of various cations on activity were examined. The comparison of kinetic data and physical properties suggested that xylanase XT and xylanase XF were identical.

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