WEKO3
アイテム
Ralstonia eutropha H16の新規細胞内3-ビドロキシ酪酸オリゴマー分解酵素(2004年度神奈川大学総合理学研究所共同研究助成論文)
http://hdl.handle.net/10487/1411
http://hdl.handle.net/10487/14115cb08265-3bf4-42d8-96c8-e9bc31c102fe
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SJKU Vol 16 2005 67-71.pdf (564.6 kB)
|
|
| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2009-02-23 | |||||
| タイトル | ||||||
| タイトル | Ralstonia eutropha H16の新規細胞内3-ビドロキシ酪酸オリゴマー分解酵素(2004年度神奈川大学総合理学研究所共同研究助成論文) | |||||
| 言語 | ||||||
| 言語 | jpn | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | Ralstonia eutropha H16 | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | poly(3-hydroxybutyrate) | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | PHB | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | intracellular 3HB-oligomer hydrolase | |||||
| 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 | departmental bulletin paper | |||||
| 著者 |
小林, 照幸
× 小林, 照幸× Kobayashi, Teruyuki× 内野, 圭一× Uchino, Keiichi× 安部, 智子× Abe, Tomoko× 齊藤, 光實× Saito, Terumi |
|||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Ralstonia eutropha H16 mobilizes intracellularly accumulated poly(3-hydroxybutyrate) with intracellular poly(3-hydroxybutyrate) depolymerases. Different types of depolymerase, PhaZ1 and its homologs, account for the mobilization significantly but incompletely, and it is proposed that further unknown depolymerases or related enzymes complement the mobilization. A novel hydrolase was therefore investigated. The amino acid sequence of the intracellular 3HB-oligomer hydrolase of Acidovoraxsp. SA1 and the genome sequence of Ralstonia solanacearum, a close relative of R. eutropha, revealed a candidate for the hydrolase gene. The DNA sequence of its hydrolase was used for the design of a pair of primes. With chromosomal DNA of R. eutropha as a template, these primers were used to amplify about a 1.3-kbp fragment including the equivalent gene, phaZc. Then the phaZc gene was cloned by Southern hybridization using the amplified DNA fragment as a probe. The hydrolase (PhaZc) was purified from Escherichia coli overexpressing phaZc and characterized. Immunoblot analysis revealed that PhaZc exists mainly in the cytosolic fraction of R. eutropha. PhaZc degraded various 3-hydroxybutyrate-oligomers at a high rate and artificial amorphous poly (3-hydroxybutyrate) at a lower rate. A phaZ-rmLl mutation enhanced the deposition of PHB in the logarithmic phase in a nutrient-rich medium. PhaZc differs from the previously reported hydrolases in R. eutropha and is a novel type of intracellular 3HB-oligomer hydrolase, which participates in the mobilization of PHB along with other hydrolases. | |||||
| 書誌情報 |
Science Journal of Kanagawa University 巻 16, p. 67-71, 発行日 2005-05-25 |
|||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 1880-0483 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA12068302 | |||||
| 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 | |||||
| その他の言語のタイトル | ||||||
| その他のタイトル | Novel intracellular 3-hydroxybutyrate-oligomer hydrolase in Ralstonia eutropha H16 | |||||
| 出版者 | ||||||
| 出版者 | 神奈川大学 | |||||
