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: Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237.
    Author: Hakamada Y, Koike K, Yoshimatsu T, Mori H, Kobayashi T, Ito S.
    Journal: Extremophiles; 1997 Aug; 1(3):151-6. PubMed ID: 9680321.
    Abstract:
    Thermostable alkaline cellulase (endo-1,4-beta-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-terminal amino acid sequence of the purified enzyme was Glu-Gly-Asn-Thr-Arg-Glu-Asp-Asn-Phe-Lys-His-Leu-Leu-Gly-Asn-Asp-Asn-Val- Lys-Arg. The enzyme had a molecular mass of approximately 86 kDa and an isoelectric point of pH 3.8. The enzyme had a pH optimum of 8.6-9.0 and displayed maximum activity at 45 degrees C. The alkaline enzyme was stable up to 50 degrees C and more than 30% of the original activity was detectable after heating at 100 degrees C and at pH 9.0 for 10 min. The enzyme hydrolyzed carboxymethylcellulose, lichenan (beta-1,3;1,4-linkage), and p-nitrophenyl derivatives of cellotriose and cellotetraose. Crystalline forms of cellulose (Avicel and filter paper), H3PO4-swollen cellulose, NaOH-swollen cellulose, curdlan (beta-1,3-linkage), laminarin (beta-1,3;1,6-linkage), and xylan were barely hydrolyzed at all.
    [Abstract] [Full Text] [Related] [New Search]