2002 Fiscal Year Final Research Report Summary
Characterization of novel viral enzymes to be utilized in recycling of biomass
| Project/Area Number |
13660094
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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 |
応用微生物学・応用生物化学
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| Research Institution | HIROSHIMA UNIVERSITY |
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Principal Investigator |
YAMADA Takashi Graduate School of ADSM, Dept. No1. Biotechnology, Professor, 大学院・先端物質科学研究科, 教授 (40230461)
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| Co-Investigator(Kenkyū-buntansha) |
FUJIE Makoto Graduate School of ADSM, Dept. No1. Biotechnology, Research Professor, 大学院・先端物質科学研究科, 助手 (20274110)
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| Project Period (FY) |
2001 – 2002
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| Keywords | chlorovirus / biomass-degradation / chitinase / chitosanase / polyuronate-degrading enzyme / ??-1, 3-glucanase |
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| Research Abstract |
Polysaccharide-degrading enzymes including chariness, chitosanases, β-1, 3-glucanse, vAL-1, and vAL-2 are encoded by chloroviruses (Phycodnaviridae). These enzymes are expressed during infection and function at the initial stage as well as the final stage of the viral replication cycle. The vChti-1 chitinase of CVK2, a virus isolated in Kyoto, Japan, has a tandem array of two catalytic domains, each of which shows a different fashion of enzyme activity. Two size-different vChta-1 chitosanases are produced from a single gene by a read-through mechanism: the larger protein with a virion-targetting signal is incorporated into the virus particle, functioning at the beginning of the infection while the smaller protein is expressed late in infection and aids in the digestion of the host cell wall prior to the release of the viruses. The cAL-1 algal lytic enzyme digests the Chlorella cell wall, releasing acidic sugars, probably uronic acids. All of these enzymes are supposed to function cooperatively to digest complex structures and compositions of the host Chlorella cell wall.
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