RESEARCH STUDY ON THE DISTRIBUTION OF D-AMINO ACIDS AND D-AMINO ACID RACEMASE IN MICROALGAE
Project/Area Number |
12660189
|
Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Fisheries chemistry
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Research Institution | Kitasato University |
Principal Investigator |
NAGAHISA Eizo School of Fisheries Sciences, KITASATO University, Professor, 水産学部, 教授 (50228053)
|
Co-Investigator(Kenkyū-buntansha) |
YOKOYAMA Takehiko Assistant Prof., 水産学部, 助手 (60296431)
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Project Period (FY) |
2000 – 2002
|
Project Status |
Completed (Fiscal Year 2002)
|
Budget Amount *help |
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2002: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2001: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2000: ¥1,300,000 (Direct Cost: ¥1,300,000)
|
Keywords | phytoplankton / microalgae / D-amino cid / D-aspartate / D-alanine / alanine racemase / autotroph / formation system / 遊離アミノ酸 / 結合型アミノ酸 / 珪藻 |
Research Abstract |
Distribution of free and combined D-amino acids in marine diatoms and freshwater microalgae was measured. And variation in D-amino acids content under various culture conditions of diatom, Asterionella sp. was examined. Furthermore, the origin of D-amino acids in microalgae was researched. 1. The presence of free D-aspartate and D-alanine was verified in diatoms, Asterionella sp., Thalassiola sp., Nitzschia sp., and Pseudo-nitzschia sp. D-Aspartate was also found in fresh water microalgae, Botrydiopsos alpina, Chlorella pyeniodos, C.vulgaris and Scenedesumus obliquus, but D-alanine was not detected in these species. 2. The content of D-alanine varied by growth phase : D-Alanine content of Asterionella sp. increased in stationary phase and decreased in extinction phase. 3. Combined form of D-aspartate, D-glutamate and D-alanine were detected in the residue of diatoms after extracting with 80% ethanol, but D-alanine was not detected in freshwater microalgae. 4. Alanine racemase activity was detected in the marine diatom, Thalassiosira sp. which was cultured germ-free. Optimal pH of this enzyme was extremely high, about 9.5 and the Km value (substrate L-alanine) was 19.7 mM. The enzyme did not require pyridoxal 5'-phosphate (PLP) as a cofactor in the reaction. These results suggest that alanine racemase from Thalassiosira sp. bindes PLP more tightly as a cofactor compared with bacterial enzyme.
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Report
(4 results)
Research Products
(3 results)
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[Publications] Yokoyama, T., Kan-no, N., Ogata, T., Kotaki, Y., Sato, M., Nagahisa, E: "Presence of free D-amino acids in and Microalgae"Biosci.Biotechnol.Biochem.. 67(2). 388-392 (2003)
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