Studies on the Xylanase from Streptomyces

Xylanase from Streptomyces xylophagus nov. sp. has been purified by ammonium sulfate fractionation and chromatography on DEAE-cellulose column. The purification of the enzyme was 276-fold with a yield of 18.6% on the basis of the activity per weight of total nitrogen. The purified enzyme was homogeneous on moving-boundary electrophoresis. Optimum pH and temperature for the enzyme activity were 6.2 and 55~60°C, respectively. The enzyme was stable up to 40°C and in the range of pH from 5.3 to 7.3, but inactivated at higher than 50°C and at extreme pH values of 2.4 and 9.4. Hydrolyzed products of xylan by the enzyme were xylose and xylobiose.