Structure and Functions of Polysaccharide-degrading Enzyme with High Activity under Extreme Environments
| Project/Area Number |
07650952
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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 |
生物・生体工学
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| Research Institution | TOKYO INSTITUTE OF TECHNOLOGY |
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Principal Investigator |
NAKAMURA Satoshi TOKYO INSTITUTE OF TECHNOLOGY,Biosci.& Biotech., Assistant Professor, 生命理工学部, 助教授 (50227899)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥2,500,000 (Direct Cost: ¥2,500,000)
Fiscal Year 1996: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1995: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Extremophile / Alkaline Enzyme / Xylanase / Gene Cloning / Protein Engineering / 極限微生物 / アルカリキシラナーゼ |
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| Research Abstract |
beta-1,4-Xylans are heterogeneous polysaccharides that have a backbone of beta-1,4-linked xylopyranose units. Xylanases catalyze the hydrolysis of xylan to xylooligosaccharides and xylose. Recently, The head investigator has isolated alkaliphilic Bacillus sp.strain 41M-1 from soil. Strain 41M-1 secreted a novel alkaline xylanase that had an alkaline pH optimum. The objective of this study is to elucidate the mechanism of xylan hydrolysis in alkaline conditions and to engineer the enzyme molecules for more extremophilic properties, such as alkaliphily. The head investigator cloned and sequenced the xylanase gene from strain 41M-1. The deduced amino acid sequence revealed that the xylanase consisted of an N-terminal catalytic domain and an additional functionally-unknown polypeptide region at the C-terminus. Glu-93 and Glu-183 in the catalytic domain, as well as Trp-18, Trp-86, Tyr-84 and Tyr-95, were involved in catalysis. Furthermore, the C-terminal region of the xylanase proved to be a polysaccharide-binding domain.
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Report
(3 results)
Research Products
(18 results)
