Purification and properties of extracellular xylan hydrolases ofStreptomyces exfoliatus

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Abstract
Fractionation of extracellular xylan hydrolases of a strain ofStreptomyces exfoliatus MC1 (by salting out, molecular sieving and ion exchange chromatography) revealed the presence of five species of the enzyme. Three major fractions could be purified to homogeneity; two were apparently endohydrolases and the third an exo-xylan hydrolase. The three fractions showed different degrees of affinity to the substrate and differed considerably in their substrate specificities. One of the endo-enzymes was specific to xylan while the other could also attack cellulose, inulin and pectin. The exo-enzyme showed xylanolytic and cellulolytic functions only. The three fractions further differed in their response to the presence of metal ions, mercapto reagents and compounds. Although the pH and temperature optima were different, the three fractions functioned synergistically in the hydrolysis of xylan.