These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and characterization of xylanase from Aspergillus ficuum AF-98.
    Author: Lu F, Lu M, Lu Z, Bie X, Zhao H, Wang Y.
    Journal: Bioresour Technol; 2008 Sep; 99(13):5938-41. PubMed ID: 18068974.
    Abstract:
    The purification and characterization of xylanase from Aspergillus ficuum AF-98 were investigated in this work. The extracellular xylanase from this fungal was purified 32.6-fold to homogeneity throughout the precipitation with 50-80% (NH(4))(2)SO(4), DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 chromatography. The purified xylanase (specific activity at 288.7 U/ mg protein) was a monomeric protein with a molecular mass of 35.0 kDa as determined by SDS-PAGE. The optimal temperature and pH for the action of the enzyme were at 45 degrees C and 5.0, respectively. The xylanase was activated by Cu(2+) up to 115.8% of activity, and was strongly inhibited by Hg(2+), Pb(2+) up to 52.8% and 89%, respectively. The xylanase exhibited K(m) and V(max) values of 3.267 mg/mL, 18.38 M/min/mg for beechwood xylan and 3.747 mg/mL, 11.1M/min/mg for birchwood xylan, respectively.
    [Abstract] [Full Text] [Related] [New Search]