Studies on Enzymatic Degradation Mechanism of Native Cellulose
| Project/Area Number |
01560091
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
応用生物化学・栄養化学
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| Research Institution | Shizuoka University |
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Principal Investigator |
OKADA Gentaro Fac. of Educ., Professor, 教育学部, 教授 (70021904)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1990: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1989: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Trichoderma viride / Cellulase / Cellulase System / Glycosylation / Meicelase / Multi-Enzyme System / Beta-Cellobiose / Multi-Functional Cellulase / Trichderma viride |
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| Research Abstract |
A cellulase component was extensively purified to essential homogeneity from a commercial crude cellulase preparation from Trichodema viride (Meicelase) by a multi-step procedure involving Amberlite CG-50 and DEAE-Sephadex A-50 column chromatographic fractionations, isoelectric focusing (pH 3.5 - 5) and Bio-Gel P-100 fractionation. The purified enzyme was designated as cellulase II-b, and was judged to be homogeneous on polyacrylamide gel and SDS-polyacrylamide gel as well as ampholine electrophoresis. The purified cellulase was completely free from beta-glucosidase.
The physicochemical and enzymatic properties of the purified enzymes were studied in detail. The purified cellulase II-b possessed a potent ability to produce glucose specifically from beta-D-cellobiose through enzymatic reversion and transcellobiosylation without any participation of beta-glucosidase. It was strongly suggested that cellulase II-b would play an important role in glucose production in the enzymatic degradation of native cellulose. This is the first finding that clearly demonstrates the requirement for a donor substrate with the correct anomer in an enzymatic reversion by cellulase. To date, no reports have appeared concerning this type of multi-functional cellulase.
From above results and others, we present the proposed scheme of the cooperative action by cellulases from T. viride in converting native cellulose to glucose.
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Report
(3 results)
Research Products
(19 results)
