| Project/Area Number |
12460058
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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 |
食品科学・栄養科学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
UTSUMI Shigeru Graduate School of Agriculture, Professor, 農学研究科, 教授 (40111976)
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| Co-Investigator(Kenkyū-buntansha) |
ADACHI Motoyasu Graduate School of Agriculture, Research Associate, 農学研究科, 助手 (60293958)
MARUYAMA Nobuyuki Graduate School of Agriculture, Research Associate, 農学研究科, 助手 (90303908)
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| Project Period (FY) |
2000 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥11,500,000 (Direct Cost: ¥11,500,000)
Fiscal Year 2002: ¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 2001: ¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 2000: ¥7,000,000 (Direct Cost: ¥7,000,000)
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| Keywords | soybean proteins / glycinin / conglycinin / physicochemical function / X-ray crystallography / bile acid-binding ability / 肝汁酸結合能 / 乳化性 / アレルゲン性 |
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| Research Abstract |
Soybean proteins have cholesterol-lowering ability as well as physicochemical functions. Moreover, their nutritional value is superior among those of plant proteins. Therefore, it is desired to enlarge the usage of soybean proteins. For this, we have to elucidate the structure-quality (physicochemical and physiological functions) relationships at molecular level of soybean proteins. We approached to the elucidation of them as follows.
(1) X-ray crystallography of the constituent subunits of glycinin and conglycinin
The three dimensional structure of conglycinin α'core was solved at 2.3Å resolution. Bases for crystallography of proglycinin A2B1a and conglycinin αcore were established.
(2) Structure-physicochemical function relationships at subunit level of glycinin and conglycinin
Molecular species composed of a single subunit and restricted subunits were purified from mutant soybean cultivars containing such species. Analyses of their structural features and physiological functions demonstrated that they exhibit the characteristic structure-physicochemical function relationships.
(3) Identification of peptide regions contributing bile acid-binding ability of glycinin
We identified the most important region responsible for bile acid binding ability of glycinin A1aB1b by using E. coli expression system.
(4) Structure-quality relationships at molecular level of glycinin and conglycinin
We could understand deeply structure-quality relationships at molecular level of glycinin and conglycinin by protein engineering based on the results obtained by the investigations (1), (2) and (3).
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