Purification and characterization of endoxylanase Xln-2 from Aspergillus niger B03

Turkish Journal of Biology

GEORGI DOBREV¹ 

关键词: Endoxylanase;    purification;    characterization;    Aspergillus niger;    xylan;   

学科分类：生物科学（综合）

来源: Scientific and Technical Research Council of Turkey - TUBITAK

【 摘 要 】

An extracellular multiple form of endoxylanase was isolated from the xylanolytic complex of Aspergillus niger B03. The enzyme was purified to a homogenous form using ultrafiltration, anion exchange chromatography, and gel filtration. It was a nonglycosylated protein with a molecular weight of 20,000 Da as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and 21,000 Da as determined by gel filtration. The optimal pH for the enzyme action was 5.0 and the optimal temperature was 55 °C. Endoxylanase stability was significantly improved in the presence of glycerol and sorbitol. The enzyme activity was activated by Mn^{2+} and Co^{2+}, and it was inhibited by Ag^+, Cu^{2+}, Fe^{3+}, Fe^{2+}, and Pb^{2+}. The substrate specificity and the product profile of the enzyme suggested that it was an endoxylanase. The enzyme showed a synergism with another endoxylanase from Aspergillus niger B03 in xylan hydrolysis.

【 授权许可】

Unknown