Purification of xylanase produced by Bacillus pumilus

Abstract

This study was aimed at purifying xylanase produced by Bacillus pumilus. The spent medium contained 27.9 UmL-1 xylanase activity and 1.5 mgmL-1 protein. The highest specific activity (33.7 Umg-1 protein) was achieved with 50% (NH4)2SO4 saturation and the xylanase recovery was 94.8%. The dialyzed and DEAE-Sepharose purified enzyme showed 6.7-fold increase in specific activity with a yield of 84.2%. Molecular weight of the purified xylanase was 55.4 KDa. Thus B. pumilus xylanase can be purified by precipitating with 50% (NH4)2SO4 saturation and DEAE-Sepharose ion exchange chromatography.