The first thermodynamic characterization of beta-1,3-xylanase from a marine bacterium

Protein J. 2005 Nov;24(7-8):413-21. doi: 10.1007/s10930-005-7637-8.


Sequence analysis of beta-1,3-xylanase (TxyA) from a marine bacterium, Alcaligenes sp. strain XY-234 implied that an xylan-binding module belonging to carbohydrate-binding module family 31 (TxyA-CBM) is separated from a catalytic module belonging to glycosyl hydrolase family 26 (TxyA-CM) by a putative glycine-rich linker [Okazaki, F., et al. (2002) J. Bacteriol. 184: 2399-2403]. In order to reveal the role of these structural features of TxyA, two modules, TxyA-CBM and TxyA-CM, were constructed, and those modules and full-length TxyA were characterized by thermodynamic studies. TxyA-CBM and TxyA-CM showed full reversible folding from denaturant-induced unfolded forms, exhibited higher thermodynamic stabilities. The conformational stability of both truncated modules is industrially desirable, as well as aiding the understanding of the enzymatic characterization of the two modules of beta-1,3-xylanase separated by a long linker.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcaligenes / enzymology*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Carbohydrates / chemistry
  • Circular Dichroism
  • Endo-1,4-beta Xylanases / chemistry*
  • Endo-1,4-beta Xylanases / metabolism
  • Guanidine / chemistry
  • Oceans and Seas
  • Protein Conformation
  • Protein Denaturation
  • Thermodynamics


  • Bacterial Proteins
  • Carbohydrates
  • Endo-1,4-beta Xylanases
  • Guanidine