『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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審査 (推奨): Peer Review [継承]
カテゴリ (推奨): 研究 [継承]
共著種別 (推奨): 国内共著 (徳島大学内研究者と国内(学外)研究者との共同研究 (国外研究者を含まない)) [継承]
学究種別 (推奨):
組織 (推奨):
著者 (必須): 1. (英) Ohshida Tatsuya (日) (読)
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2.林 順司 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.食料科学系.食料科学分野]/[徳島大学.生物資源産業学部.生物資源産業学科.食料科学講座])
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3. (英) Satomura Takenori (日) (読)
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4.川上 竜巳 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.食料科学系.食料科学分野]/[徳島大学.生物資源産業学部])
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5.大島 敏久 ([九州大学])
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6.櫻庭 春彦
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題名 (必須): (英) First characterization of extremely halophilic 2-deoxy-D-ribose-5-phosphate aldolase  (日)    [継承]
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要約 (任意): (英) 2-Deoxy-d-ribose-5-phosphate aldolase (DERA) catalyzes the aldol reaction between two aldehydes and is thought to be a potential biocatalyst for the production of a variety of stereo-specific materials. A gene encoding DERA from the extreme halophilic archaeon, Haloarcula japonica, was overexpressed in Escherichia coli. The gene product was successfully purified, using procedures based on the protein's halophilicity, and characterized. The expressed enzyme was stable in a buffer containing 2 M NaCl and exhibited high thermostability, retaining more than 90% of its activity after heating at 70 °C for 10 min. The enzyme was also tolerant to high concentrations of organic solvents, such as acetonitrile and dimethylsulfoxide. Moreover, H. japonica DERA was highly resistant to a high concentration of acetaldehyde and retained about 35% of its initial activity after 5-h' exposure to 300 mM acetaldehyde at 25 °C, the conditions under which E. coli DERA is completely inactivated. The enzyme exhibited much higher activity at 25 °C than the previously characterized hyperthermophilic DERAs (Sakuraba et al., 2007). Our results suggest that the extremely halophilic DERA has high potential to serve as a biocatalyst in organic syntheses. This is the first description of the biochemical characterization of a halophilic DERA.  (日)    [継承]
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誌名 (必須): Protein Expression and Purification ([Elsevier])
(pISSN: 1046-5928, eISSN: 1096-0279)

ISSN (任意): 1096-0279
ISSN: 1046-5928 (pISSN: 1046-5928, eISSN: 1096-0279)
Title: Protein expression and purification
Title(ISO): Protein Expr Purif
Publisher: Elsevier Inc.
 (NLM Catalog  (Scopus  (CrossRef (Scopus information is found. [need login])
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(必須): 126 [継承]
(必須): [継承]
(必須): 62 68 [継承]
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年月日 (必須): 西暦 2016年 5月 20日 (平成 28年 5月 20日) [継承]
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DOI (任意): 10.1016/j.pep.2016.05.009    (→Scopusで検索) [継承]
PMID (任意): 27215670    (→Scopusで検索) [継承]
NAID (任意):
WOS (任意): 000380579400009 [継承]
Scopus (任意): 2-s2.0-84973496063 [継承]
機関リポジトリ : 111972 [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1016/j.pep.2016.05.009  (日)    [継承]
2.(英) Article.ELocationID: S1046-5928(16)30087-0  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]
4.(英) KeywordList.Keyword: 2-Deoxy-d-ribose-5-phosphate aldolase  (日)    [継承]
5.(英) KeywordList.Keyword: Aldehyde  (日)    [継承]
6.(英) KeywordList.Keyword: Archaea  (日)    [継承]
7.(英) KeywordList.Keyword: Haloarcula japonica  (日)    [継承]
8.(英) KeywordList.Keyword: Halophile  (日)    [継承]
9.(英) KeywordList.Keyword: Organic solvent  (日)    [継承]

標準的な表示

和文冊子 ● Tatsuya Ohshida, Junji Hayashi, Takenori Satomura, Ryushi Kawakami, Toshihisa Ohshima and Haruhiko Sakuraba : First characterization of extremely halophilic 2-deoxy-D-ribose-5-phosphate aldolase, Protein Expression and Purification, Vol.126, 62-68, 2016.
欧文冊子 ● Tatsuya Ohshida, Junji Hayashi, Takenori Satomura, Ryushi Kawakami, Toshihisa Ohshima and Haruhiko Sakuraba : First characterization of extremely halophilic 2-deoxy-D-ribose-5-phosphate aldolase, Protein Expression and Purification, Vol.126, 62-68, 2016.

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