The thermostabilizing domain, XynA, of Caldibacillus cellulovorans xylanase is a xylan binding domain

Biochem J. 2000 Mar 15;346 Pt 3(Pt 3):583-6.

Abstract

We show that the N-terminal 'thermostabilizing domain' (TSD) of the xylanase, XynA, from the thermophilic bacterium Caldibacillus cellulovorans also acts as a xylan binding domain. Affinity electrophoresis experiments show that this TSD selectively binds soluble xylan and binds weakly to hydroxyethylcellulose. Based on this, and previously reported evidence, we propose that xylanase-associated TSDs are xylan binding domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Clostridium / enzymology*
  • DNA Primers
  • Electrophoresis, Polyacrylamide Gel / methods
  • Endo-1,4-beta Xylanases
  • Molecular Sequence Data
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Temperature
  • Xylans / metabolism*
  • Xylosidases / chemistry
  • Xylosidases / isolation & purification
  • Xylosidases / metabolism*

Substances

  • DNA Primers
  • Xylans
  • Xylosidases
  • Endo-1,4-beta Xylanases