Novel glycoside hydrolases identified by screening a Chinese Holstein dairy cow rumen-derived metagenome library

Appl Environ Microbiol. 2010 Oct;76(19):6701-5. doi: 10.1128/AEM.00361-10. Epub 2010 Aug 13.

Abstract

One clone encoding glycoside hydrolases was identified through functional screening of a rumen bacterial artificial chromosome (BAC) library. Of the 68 open reading frames (ORFs) predicted, one ORF encodes a novel endo-β-1,4-xylanase with two catalytic domains of family GH43 and two cellulose-binding modules (CBMs) of family IV. Partial characterization showed that this endo-xylanase has a greater specific activity than a number of other xylanases over a wide temperature range at neutral pH and could be useful in some industrial applications.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cattle / microbiology*
  • China
  • Chromosomes, Artificial, Bacterial
  • Cloning, Molecular / methods
  • Endo-1,4-beta Xylanases / chemistry
  • Endo-1,4-beta Xylanases / genetics*
  • Endo-1,4-beta Xylanases / metabolism*
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Metagenome*
  • Molecular Sequence Data
  • Open Reading Frames
  • Protein Structure, Tertiary
  • Rumen / microbiology*
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Substrate Specificity
  • Temperature

Substances

  • Endo-1,4-beta Xylanases