Elucidation of cellobiose metabolic pathway in Trichoderma reesei
| Project/Area Number |
21612002
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biomass energy
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| Research Institution | Nagaoka University of Technology |
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Principal Investigator |
OKADA Hirofumi 長岡技術科学大学, 工学部, 准教授 (70233343)
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| Co-Investigator(Renkei-kenkyūsha) |
OGASAWARA Wataru 長岡技術科学大学, 工学部, 准教授 (40292172)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2011: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2010: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2009: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 遺伝子 / 応用微生物 / 菌類 / 酵素 / バイオマス / β-グルコシダーゼ / セルロース / セロビオース |
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| Research Abstract |
Trichoderma reesei, which is well known to produce large amount of cellulases, expresses threeβ-glucosidases(BGLs), one of which is secreted Cel3A and the other are intracellular Cel1A and Cel3C, when grown on cellulose. To elucidate the physiological roles of these BGLs, we investigated the enzymatic properties of the recombinant enzymes produced by heterologous hosts. Furthermore, we constructed the deficient mutants of the corresponding BGL genes and characterized the amount of biomass and the cellulase and BGL activities of the mutants when grown on cellulose or cellobiose. The results demonstrated that Cel3A and Cel3C preferred pNP-Glc to cellobiose as the substrate, whereas Cel1A had higher activity for cellobiose than that for pNP-Glc. The intracellular and extracellular BGL activities of the mutants reflected the substrate specificity of the respective enzymes. We assumed that Cel1A plays the key role in cellobiose metabolism and the BGLs would not directly involve in cellulase induction. When T. reesei is grown on cellobiose, the other BGL(s) besides Cel3A seems to be expressed and secreted.
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Report
(4 results)
Research Products
(10 results)
