| Project/Area Number |
15H06898
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Okazaki Research Facilities, National Institutes of Natural Sciences |
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Principal Investigator |
NAKAMURA Akihiko 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 助教 (20752968)
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| Project Period (FY) |
2015-08-28 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | セルラーゼ / 一分子観察 / キネティクス / セルロース / 糖鎖修飾 / モータータンパク / X線構造解析 / バイオマス |
|---|
| Outline of Final Research Achievements |
Cellulase from fungi (TrCel6A) and bacteria (CfCel6B) is constructed by catalytic domain, binding domain and linker region, connecting the two domains. But each domain has different structure between the two enzymes. Therefore the role of domains on cellulose binding, dissociation and hydrolysis were compared between TrCel6A and CfCel6B by single fluorescence observation. For TrCel6A, glycosylated linker region and binding domain were important for binding and specificity for binding surface respectively. In contrast, binding domain of CfCel6B showed high binding rate and specificity. Additionally, catalytic domain of CfCel6B showed processive movement on cellulose but that of TrCel6A was not observed. This difference might be caused by the difference of length of loop region covering the catalytic site.
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