Molecular cloning, nucleotide sequence and characteristics of a xylanase gene (xynA) from Ruminococcus albus 7

Mutsumi Nakamura, Takafumi Nagamine, Akio Takenaka, Rustam Aminov, Koretsugu Ogata, Kiyoshi Tajima, Hiroki Matsui, Yoshimi Benno, Hisao Itabashi

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Abstract

A 2.6‐kb DNA fragment encoding a xylanase gene (xynA) was cloned from the rumen hemicellulolytic bacterium Ruminococcus albus 7. The deduced primary structure of the protein (XynA) was divided into a signal peptide region and 3 domains. Domain A was identified as a family 11 (G) catalytic domain, but one amino acid residue was replaced by another in an active site signature 1 of family 11. Domain B is a stabilizing domain for the catalytic domains of families 10 and 11. Deletion of domain B reduced stability of the xylanase at high temperature and at high and low pH. Domain B may be useful for protein engineering of xylanase. Domain C has sequence similarity to deacetylases and NodB proteins.
Original languageEnglish
JournalAnimal Science Journal
Volume73
Issue number5
Pages (from-to)347-352
Number of pages6
ISSN1344-3941
DOIs
Publication statusPublished - 2002
Externally publishedYes

Keywords

  • fiber digestion
  • hemicellulose
  • rumen bacteria
  • Ruminococcus albus
  • xylanase gene

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