The global analysis of the chitinolytic system of the marine bacterium
| Project/Area Number |
24580309
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Fisheries chemistry
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| Research Institution | Osaka University of Pharmaceutical Sciences |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2014: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
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| Keywords | キチナーゼ / N-アセチルグルコサミニダーゼ / キチン結合タンパク質 / NagR / バイオマス / キチン分解細菌 |
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| Outline of Final Research Achievements |
We have clarified that four chitinases (ChiA, ChiB, ChiC, and ChiD), three β-N-acetylglucosaminidases (GlcNAcases A, B, and C), a transglycosylative enzyme (Hex99), a chitin-binding protein (Cbp1), and two proteases (AprIV and MprIII) are involved in chitin degradation of the marine bacterium, Pseudoalteromonas piscicida strain O-7. Recently, the genome analysis of this strain was performed by Illumina Genome Analyzer. The homology search indicated that there are additional chitinases-, chitin-binding protein-, and N-acetylglucosaminidase-encoding genes in the genome. Real-time quantitative PCR analyses demonstrated that the expression of these genes was induced by the presence of N-acetylglucosamine. The proteins were produced in E. coli BL21 (DE3) and purified with Ni Sepharose Fast Flow (GE Healthcare). The function of each protein has been examined. Furthermore, NagR homologs of P. piscicida strain O-7 were also produced.
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Report
(4 results)
Research Products
(24 results)
