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

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Abstract

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.

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Abbreviations

CBM:

carbohydrate-binding module

CM:

catalytic module

Gdn-HCl:

guanidine hydrochloride

TX:

β-1,3-xylan

TxyA:

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

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Authors and Affiliations

  1. School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST), 1-1 Asahidai, Nomi, Ishikawa, 923-1292, Japan

    Fumiyoshi Okazaki & Masahiro Takagi

  2. Institute of Applied Physics, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8573, Japan

    Kentaro Shiraki

  3. Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, Mie, 514-8507, Japan

    Yutaka Tamaru & Toshiyoshi Araki

Authors
  1. Fumiyoshi Okazaki
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  2. Kentaro Shiraki
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  3. Yutaka Tamaru
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  4. Toshiyoshi Araki
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  5. Masahiro Takagi
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Correspondence to Masahiro Takagi.

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Okazaki, F., Shiraki, K., Tamaru, Y. et al. The First Thermodynamic Characterization of β-1,3-Xylanase from a Marine Bacterium. Protein J 24, 413–421 (2005). https://doi.org/10.1007/s10930-005-7637-8

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  • DOI: https://doi.org/10.1007/s10930-005-7637-8

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