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: Characterization of a thermostable endo-1,5-alpha-L-arabinanase from Caldicellulorsiruptor saccharolyticus.
    Author: Hong MR, Park CS, Oh DK.
    Journal: Biotechnol Lett; 2009 Sep; 31(9):1439-43. PubMed ID: 19458916.
    Abstract:
    A recombinant putative glycoside hydrolase from Caldicellulosiruptor saccharolyticus was purified with a specific activity of 12 U mg(-1) by heat treatment and His-Trap affinity chromatography, and identified as a single 56 kDa band upon SDS-PAGE. The native enzyme is a dimer with a molecular mass of 112 kDa as determined by gel filtration. The enzyme exhibited its highest activity when debranched arabinan (1,5-alpha-L-arabinan) was used as the substrate, demonstrating that the enzyme was an endo-1,5-alpha-L-arabinanase. The K (m), k (cat), and k (cat)/K (m) values were 18 mg ml(-1), 50 s(-1), and a 2.8 mg ml(-1) s(-1), respectively. Maximum enzyme activity was at pH 6.5 and 75 degrees C. The half-lives of the enzyme at 65, 70 and 75 degrees C were 2440, 254 and 93 h, respectively, indicating that it is the most thermostable of the known endo-1,5-alpha-L-arabinanases.
    [Abstract] [Full Text] [Related] [New Search]