Turkish Journal of Biology
DOI
10.3906/biy-1101-189
Abstract
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.
Keywords
Endoxylanase, purification, characterization, Aspergillus niger, xylan
First Page
7
Last Page
13
Recommended Citation
DOBREV, GEORGI and ZHEKOVA, BORIANA
(2012)
"Purification and characterization of endoxylanase Xln-2 from Aspergillus niger B03,"
Turkish Journal of Biology: Vol. 36:
No.
1, Article 2.
https://doi.org/10.3906/biy-1101-189
Available at:
https://journals.tubitak.gov.tr/biology/vol36/iss1/2