| Project/Area Number |
08456168
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
生物資源科学
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| Research Institution | Toyama Prefectural University (1997-1998)
University of Fukui (1996) |
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Principal Investigator |
ITOH Nobuya Toyama Prefectural University, Professor, 工学部, 教授 (90213066)
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| Project Period (FY) |
1996 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 1998: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1997: ¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 1996: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | bromoform / monohalomethane / bromoperoxidase / SAM ; halide ion methyl transferase / marine algae / allelochemical / アレロケミカル / SAM:ハライドイオンメチル転移酵素 / トリハロメタン / 海洋生物 / 細菌 / ハロペルオキシダーゼ / 臭化メチル / SAM-ハライドイオンメチル転移酵素 |
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| Research Abstract |
Bromoform produced by some marine algae including Corallina was found to be a kind of allelochemical eliminating the epiphytic organisms, especially, diatoms on the algal surface.
On the other hand, monohalomethanes have been observed to emit from some marine macro- and microalgae such as Paviova sp. Molecular characterization to form monohalomethanes in these algae have revealed that SAM : halide ion methyltransferase reaction participates in the reaction. However, these enzymes were very unstable, therefaore, further characterization had been difficult. Recently, we have found a marine microalga having the relatively stable enzyme and established the purification procedures to isolate it. This is the first work to purify the SAM : halide ion methyltransferase from marine microalga. The emission of methyl bromide from marine environment, especially from marine microalgae, could explain the amount of methyl bromide in the atmosphere.
In this research project, we have cloned the gene encoding a novel Co^<2+>-activating bromoperoxidase from a soil microorganism, Pseudomonas putida. The recombinant enzyme catalyzed the brominating reactions of styrene and indene giving the corresponding racemic bromohydrin compounds. It was also found that the enzyme has a esterase activity toward methyl D-acethylthioisobutyrate, suggesting that the enzyme is an unique bifunctional enzyme.
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