The Protein Journal

, Volume 24, Issue 7–8, pp 413–421 | Cite as

The First Thermodynamic Characterization of β-1,3-Xylanase from a Marine Bacterium

  • Fumiyoshi Okazaki
  • Kentaro Shiraki
  • Yutaka Tamaru
  • Toshiyoshi Araki
  • Masahiro TakagiEmail author


Sequence analysis of β-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 β-1,3-xylanase separated by a long linker.


β-1-3-Xylanase carbohydrate-binding module family 31 glycosyl hydrolase family 26 thermodynamic stability 



carbohydrate-binding module


catalytic module


guanidine hydrochloride




β-1,3-xylanase from a marine bacterium, Alcaligenes sp. strain XY-234.


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Copyright information

© Springer Science+Business Media, Inc. 2005

Authors and Affiliations

  • Fumiyoshi Okazaki
    • 1
  • Kentaro Shiraki
    • 2
  • Yutaka Tamaru
    • 3
  • Toshiyoshi Araki
    • 3
  • Masahiro Takagi
    • 1
    Email author
  1. 1.School of Materials ScienceJapan Advanced Institute of Science and Technology (JAIST)Nomi, IshikawaJapan
  2. 2.Institute of Applied PhysicsUniversity of TsukubaTsukuba, IbarakiJapan
  3. 3.Department of Life ScienceFaculty of Bioresources, Mie UniversityTsu, MieJapan

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