| Title |
The First Thermodynamic Characterization of β-1,3-Xylanase from a Marine Bacterium
|
|---|---|
| Published in |
The Protein Journal, November 2005
|
| DOI | 10.1007/s10930-005-7637-8 |
| Pubmed ID | |
| Authors |
Fumiyoshi Okazaki, Kentaro Shiraki, Yutaka Tamaru, Toshiyoshi Araki, Masahiro Takagi |
| Abstract |
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. |
Mendeley readers
The data shown below were compiled from readership statistics for 16 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 16 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Master | 3 | 19% |
| Student > Ph. D. Student | 3 | 19% |
| Lecturer | 1 | 6% |
| Student > Bachelor | 1 | 6% |
| Other | 1 | 6% |
| Other | 3 | 19% |
| Unknown | 4 | 25% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 6 | 38% |
| Biochemistry, Genetics and Molecular Biology | 3 | 19% |
| Physics and Astronomy | 1 | 6% |
| Engineering | 1 | 6% |
| Unknown | 5 | 31% |
Attention Score in Context
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 31 August 2013.
All research outputs
#8,534,976
of 25,374,647 outputs
Outputs from The Protein Journal
#163
of 639 outputs
Outputs of similar age
#26,896
of 76,667 outputs
Outputs of similar age from The Protein Journal
#1
of 1 outputs
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