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: Production, purification, and characterization of a cellulase-free thermostable endo-xylanase from Thermoanaerobacterium thermosaccharolyticum DSM 571.
    Author: Li X, Shi H, Ding H, Zhang Y, Wang F.
    Journal: Appl Biochem Biotechnol; 2014 Dec; 174(7):2392-402. PubMed ID: 25261357.
    Abstract:
    This is the first report describing the cloning, expression, and characterization of a putative thermostable, cellulase-free xylanase (XYN) from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum DSM 571. The temperature and pH values for optimal enzyme activity of XYN were found to be 65 °C and pH 6.5, respectively. The XYN activity was apparently enhanced by Co(2+), Mn(2+), and Tween 60 and significantly inactivated by Al(3+), Cu(2+), Zn(2+), and SDS. The K m and V max values of XYN for the hydrolysis of beechwood xylan were 2.1 mg/ml and 222.1 U/mg, respectively. The k cat values of XYN for beechwood xylan at the optimal temperature and pH values were 481.4 s(-1). XYN represents an attractive candidate for use in the large-scale production of xylooligosaccharides (XOs) from forest residues because it is an endo-xylanase capable of degrading xylan.
    [Abstract] [Full Text] [Related] [New Search]