2007 Fiscal Year Final Research Report Summary
Efficient carbon dioxide fixation by aromaticcarboxylate decarboxylases catalyzing carboxylation reactions
| Project/Area Number |
18580072
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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 |
Applied microbiology
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| Research Institution | Gifu University |
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Principal Investigator |
YOSHIDA Toyokazu Gifu University, Department of Engineering, Associate Professor (90220657)
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| Co-Investigator(Kenkyū-buntansha) |
NAGASAWA Toru Gifu University, Department of Engineering, Professor (60115904)
MITSUKURA Koichi Gifu University, Department of Engineering, Reseatch Assistant (70324283)
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| Project Period (FY) |
2006 – 2007
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| Keywords | Enzymatic reaction / Applied microbiology / Enzyme / Bioreactor / Biological function |
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| Research Abstract |
Various enzymes catalyzing oxidative or nonoxidative decarboxylation reaction are involved in aerobic or anaerobic degradation of aromatic carboxylic acids in microorganisms. Recently, we found and characterized several kinds of novel decarboxylase, catalyzing the reverse carboxylation reaction efficiently. In the present study, we surveyed and characterized 2,3 and 3,4 dihydroxybenzoate decarboxylases. The decarboxylases were purified to homogeneity, and physicochemicarl properties were investigated. Both dacarboxylases catalyzed the reverse carboxylation reactions for catechol as a substrate. The decarboxylases genes were cloned and analyzed. The decarboxylases were classified into independent enzyme groups on the basis of their primary structures. Furthermore, we surveyed heat stable reversible decarboxylases for the application to enzymatic carbon dioxide fixation in supercritical carbon dioxide. In supercritical carbon dioxide, pH shift and temperature affected the carboxylation activity of decarboxylases severely. From enrichment cultures using 4-hydroxybenzoic acid as a sole carbon source, microorganisms possessing heat-stable 4-hydroxybenzoate decarboxylases have been isolated.
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Research Products
(12 results)
