Analysis of the glycosidases on the metabolism of arabinogalactan-protein in Bifidobacteria
| Project/Area Number |
24580144
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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 |
Applied biochemistry
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| Research Institution | Kagoshima University |
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Principal Investigator |
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| Research Collaborator |
SHIMOKAWA Michiko
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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: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 糖質分解酵素 / プレバイオティクス / アラビノガラクタン-プロテイン / ビフィズス菌 / 腸内細菌 / Ⅱ型アラビノガラクタン / ガラクトース / アラビノース / II型アラビノガラクタン |
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| Outline of Final Research Achievements |
Type II arabinogalactan is a suitable carbohydrate source for Bifidobacterium longum, but the metabolic pathway has never been revealed. In this study, we cloned and characterized GH43 exo-β-1,3-galactanase (BLLJ_1840), GH30 β-1,6-galactanase (BLLJ_1841), and GH43 α-L-arabinofuranosidase (BLLJ_1854) from B. longum JCM1217. Furthermore, we revealed a degradation pathway for type II arabinogalactan in B. longum.
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Report
(4 results)
Research Products
(21 results)
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[Journal Article] Crystal structure of glycoside hydrolase family 127 β-L-arabinofuranosidase from Bifidobacterium longum.2014
Author(s)
Ito, T., Saikawa, K., Kim, S., Fujita, K., Ishiwata, A., Kaeothip, S., Arakawa, T., Wakagi, T., Beckham G. T., Ito, Y., and Fushinobu, S.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: in press
Related Report
Peer Reviewed
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