Purification and properties of a xylanase from Streptomyces lividans

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Abstract
An extracellular xylanase produced by a cellulase-negative mutant strain of Streptomyces lividans 1326 was purified to homogeneity. The purified enzyme has an apparent Mr of 43000 and pI of 5.2. The pH and temperature optima for the activity were 6.0 and 60.degree.C respectively, and the Km and Vmax. values, determined with a soluble oat spelts xylan, were 0.78 mg/ml and 0.85 mmol/min per mg of enzyme. The xylanase showed no activity towards CM-cellulose and p-nitrophenyl .beta.-D-xyloside. The enzyme degraded xylan, producing mainly xylobiose, a mixture of xylo-oligosaccharides and a small amount of xylose as end products. Its pattern of action on .beta.-1,4-D-xylan indicates that it is a .beta.-1,4-endoxylanase (EC 3.2.1.8).