| Project/Area Number |
11217214
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Science and Engineering
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| Research Institution | Kanagawa University |
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Principal Investigator |
SAITO Terumi Kanagawa Univ., Dept. of Science, Professor, 理学部, 教授 (80025717)
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| Co-Investigator(Kenkyū-buntansha) |
KOBAYASHI Teruyuki Kanagawa Univ., Dept. of Science, Postdoctoral, 理学部, 博士研究員
井上 和仁 神奈川大学, 理学部, 助教授 (20221088)
小笠原 強 神奈川大学, 理学部, 教授 (20167315)
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| Project Period (FY) |
1999 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥35,700,000 (Direct Cost: ¥35,700,000)
Fiscal Year 2002: ¥8,000,000 (Direct Cost: ¥8,000,000)
Fiscal Year 2001: ¥8,000,000 (Direct Cost: ¥8,000,000)
Fiscal Year 2000: ¥8,000,000 (Direct Cost: ¥8,000,000)
Fiscal Year 1999: ¥11,700,000 (Direct Cost: ¥11,700,000)
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| Keywords | poly (3-hydroxybatyrate) / polyhydroxy alkanoates / PHB depolymerase / PHB / inclusion bodies / intracellular PHB depolymerase / biodegradation / bacterial polyesters / 生分解性 / 生分解性ポリエステル / ポリ-3-ヒドロキシ酪酸 / ポリヒドロキシアルカノエート / PHA / 嫌気 / ボリヒドロキシアルカノエート |
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| Research Abstract |
Several bacteria which degrade bacterial polyester (PHB) and also perform denitrification were isolated. We attempted the isolation of extracellular PHB depolymerases and cloning of their genes, but failed. When small fish (gold fish) were kept in the presence of PHB, a considerable reduction of nigrogen compounds in water was observed. These results indicate that the important role of the bacteria with ability of both PHB-degradation and denitrification in environment. On the other hand, we coned the gene of an intracellular PHB depolymerase (phaZl) from Ralstonia eutropha H16 and charaterization its product (PhaZ1). The amino acid sequence of PhaZ1 was novel. The molecular mass of PhaZ1 was 47 Kda. PhaZ1, which localized solely in PHB inclusions, degraded artificial amorphous PHB granules, but not crystalline PHB granules. We further cloned several intracellular 3-hydroxybutyrate-oligomer hydrolases. One of them, an intracellular 3HB-oligomer hydrolase (PhaZ2) from R. eutropha, showed both 3HB-oligomer hydrolase and PHB depolymerase activities, PhaZ2 localizedd both in cytosol and PHB inclusions, The amounts of PhaZ1 and PhaZ2 increased with the content of PHB in cells. The null mutant lacking both PhaZ1and PhaZ2 revealed the increase PHB deposition in cells. These results indicate that PhaZ1 and PhazZ2 cooperate in intracellular degradation of PHB
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