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Novel thermostable glycosidases in the extracellular matrix of the terrestrial cyanobacterium Nostoc commune
http://hdl.handle.net/2297/36907
http://hdl.handle.net/2297/369070af1c23c-a3e5-43c5-b9c3-ef6a0717b8e1
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SC-PR-SAKAMOTO-T-243.pdf (606.0 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-03 | |||||
| タイトル | ||||||
| タイトル | Novel thermostable glycosidases in the extracellular matrix of the terrestrial cyanobacterium Nostoc commune | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Mohamed Morsy, Fatthy
× Mohamed Morsy, Fatthy× Kuzuha, Satomi× Takani, Yayoi× Sakamoto, Toshio |
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| 書誌情報 |
The Journal of General and Applied Microbiology 巻 54, 号 5, p. 243-252, 発行日 2008-01-01 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0022-1260 | |||||
| NCID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA00698664 | |||||
| DOI | ||||||
| 関連タイプ | isIdenticalTo | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.2323/jgam.54.243 | |||||
| 出版者 | ||||||
| 出版者 | 応用微生物学・分子細胞生物学研究奨励会 = The Applied Microbiology, Molecular and Cellular Biosciences Research Foundation | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | The cyanobacterium Nostoc commune is adapted to the terrestrial environment and forms a visible colony in which the cells are embedded in extracellular polysaccharides (EPSs), which play a crucial role in the extreme desiccation tolerance of this organism. When natural colonies were immersed in water, degradation of the colonies occurred within 2 days and N. commune cells were released into the water. The activities that hydrolyze glycoside bonds in various N. commune fractions were examined using artificial nitrophenyl-linked sugars as substrates. A β-D-glucosidase purified from the water-soluble fraction was resistant to 20 min of boiling. The β-D-glucosidase, with a molecular mass of 20 kDa, was identified as a cyanobacterial fasciclin protein based on its N-terminal amino-acid sequence. The 36-kDa major protein in the water-soluble fraction was purified, and the N-terminal amino-acid sequence of the protein was found to be identical to that of the water-stress protein (WspA) of N. commune. This WspA protein also showed heat-resistant β-D-galactosidase activity. The fasciclin protein and WspA in the extracellular matrix may play a role in the hydrolysis of the EPSs surrounding the cells, possibly as an aid in the dispersal of cells, thus expanding the colonies of this cyanobacterium. | |||||
| 権利 | ||||||
| 権利情報 | Copyright © 2009 by The Applied Microbiology, Molecular and Cellular Biosciences Research Foundation | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| 関連URI | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | https://www.jstage.jst.go.jp/browse/jgam | |||||
| 関連URI | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://www.ammcb.info/ | |||||
