| Project/Area Number |
08456067
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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 KYOTO UNIVERSITY,Research Institute for Food Science, Professor, 食糧科学研究所, 教授 (40111976)
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| Co-Investigator(Kenkyū-buntansha) |
MARUYAMA Nobuyuki KYOTO UNIVERSITY,Research Institute for Food Science, Research Asociate, 食糧科学研究所, 助手 (90303908)
ADACHI Motoyasu KYOTO UNIVERSITY,Research Institute for Food Science, Research Associate, 食糧学研究所, 助手 (60293958)
竹中 康之 京都大学, 食糧科学研究所, 助手 (20273518)
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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 |
¥8,800,000 (Direct Cost: ¥8,800,000)
Fiscal Year 1998: ¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1997: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1996: ¥5,400,000 (Direct Cost: ¥5,400,000)
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| Keywords | soybean / storage proteins / glycinin / conglycinin / X-ray crystallography / recombinant / functional properties / β-コングリシニン / 構造機能相関 |
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| Research Abstract |
Object of this project is to elucidate quality-structure relationships of soybean storage proteins glycinin and conglycinin. We approached to investigate these from three viewpoints.
(1) Structure-function relationships of glycinin : We modified glycinin to improve its functional properties based on the structure-function relationships revealed by us prior to this study. Most of the modified glycinins exhibited better functional properties than those of the native glycinin, indicating that the structure-function relationships revealed by us are reasonable.
(2) Structure-function relationships of conglycinin : F.coli expression systems for the constituent subunits alpha, alpha' and beta of conglycinin were constructed. All recombinant subunits formed homotrimers having the proper conformation. Analyses of functional properties of these recombinant subunits revealed structural factors determining their solubilities, surface hydrophobicities, heat-stabilities, emulsifying abilities and heat-induced association.
(3) X-ray crystallography of recombinant and native glycinin and conglycinin : Recombinant proglycinin A1aB1b, A3B4 and conglycinin beta prepared using B.coli expression systems, and native glycinin A3B4 and conglycinin beta prepared from mutant soybeans containing glycinin or conglycinin composed of a kind of subunit were crystallized for X-ray crystallography. Their three dimensional structures were solved at 2.1-2.8 * levels. These elucidation surely contribute to investigate quality-structure relationships of glycinin and conglycinin at a molecular level.
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