| Project/Area Number |
25820396
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biofunction/Bioprocess
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| Research Institution | Hokkaido University (2014)
Tohoku University (2013) |
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Principal Investigator |
NAKASHIMA Kazunori 北海道大学, 工学(系)研究科(研究院), 准教授 (50540358)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | バイオマス分解 / 前処理 / 融合タンパク質 |
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| Outline of Final Research Achievements |
We constructed novel fusion enzymes consisting of Bacillus subtilis expansin EXLX1 and Clostridium thermocellum endoglucanase CelD. These two components are directly fused, or fused using flexible glycine-serine peptide linkers (GGGGS, GS linker) with different lengths: a triplicate (GGGGS)3 linker (GS3) and a sextuple (GGGGS)6 linker (GS6), resulting in fusion enzymes EXLX1-CelD, EXLX1-GS3-CelD and EXLX1-GS6-CelD. The binding ability and digestibility of these fusion enzymes towards a series of cellulose substrates with different crystallinity index (CrI) was examined. Fused with EXLX1, CelD showed higher binding ability to various kinds of cellulose. In the degradation of cellulose, EXLX1-GS3-CelD exhibited the highest degradation activity among the fusion enzymes examined, suggesting that linker length between the two proteins has a significant impact on the activity of the fusion enzyme. EXLX1-GS3-CelD was found to function more effectively towards higher crystalline celluloses.
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