| Project/Area Number |
24380055
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
KANAYA SHIGENORI 大阪大学, 工学(系)研究科(研究院), 教授 (30273585)
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| Co-Investigator(Renkei-kenkyūsha) |
KOGA Yuichi 大阪大学, 大学院工学研究科, 准教授 (30379119)
CLEMENT Angkawidjaja 大阪大学, 大学院工学研究科, 特任助教 (20505987)
KANAYA Eiko 大阪大学, 大学院工学研究科, 特任研究員 (80396217)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥17,940,000 (Direct Cost: ¥13,800,000、Indirect Cost: ¥4,140,000)
Fiscal Year 2014: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
Fiscal Year 2013: ¥6,500,000 (Direct Cost: ¥5,000,000、Indirect Cost: ¥1,500,000)
Fiscal Year 2012: ¥8,060,000 (Direct Cost: ¥6,200,000、Indirect Cost: ¥1,860,000)
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| Keywords | クチナーゼ / ポリエステル / サチライシン / プリオン / カルシウム結合部位 / メタゲノム / Ｘ線結晶構造解析 / セルラーゼ / 飽和変異 / セリンプロテアーゼ / 超好熱菌 / プリオン分解 / 速度論的安定性 / ジスルフィド結合 / 菌体外漏出 / 成熟化 / X線結晶構造解析 |
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| Outline of Final Research Achievements |
The crystal structure of LC-cutinase with PET-degrading activity was determined. Then, the mutations were introduced into LC-cutinase and two proteases (Tk-subtilisin and Tk-SP) with abnormal prion-degrading activity based on their structures to improve their enzymatic properties. As a result, the LC-cutinase derivative with enhanced stability, the Tk-subtilisin derivative with increased maturation rate, and the Tk-SP derivative with high stability in the presence of EDTA were constructed. In addition, two thermostable cellulases were isolated from leaf-branch compost by a metagenomic approach and their crystal structures were determined.
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