2012 Fiscal Year Final Research Report
A research for the chitinolytic systems of bacteria
| Project/Area Number |
22580381
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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 |
Boundary agriculture
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| Research Institution | Osaka University of Pharmaceutical Sciences |
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Principal Investigator |
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| Project Period (FY) |
2010 – 2012
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| Keywords | バイオマス / 環境微生物 / 海洋細菌 / キチン |
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| Research Abstract |
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 strain O-7 was performed by Illumina Genome Analyzer. The homology search indicated that there are additional chitinase-, 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 GlcNAc. The proteins were produced in E. coli BL21 (DE3) and purified with Ni Sepharose Fast Flow (GE Healthcare).
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[Journal Article] Crystallization and preliminary X-ray crystallographic analysis of BxlA, an intracellular beta-D-xylosidase from Streptomyces thermoviolaceus OPC-5202010
Author(s)
Hideaki Morioka, Yasuhiro Miki, Kei Saito, Koji Tomoo, Toshimasa Ishida, TomokazuHasegawa, Akihito Yamano, Chiaki Takada, Katsushiro Miyamoto, and Hiroshi Tsujibo
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Journal Title
Acta Crystallogr Sect F Struct Biol Cryst Commun
Volume: 66
Pages: 791-793
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