1995 Fiscal Year Final Research Report Summary
Functional properties and conformational changes of food proteins - Roles of molten globule state
| Project/Area Number |
05453170
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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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 |
HIROSE Masaaki Kyoto University, Research Institute for Food Science, Professor, 食糧科学研究所, 教授 (60026523)
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| Co-Investigator(Kenkyū-buntansha) |
YAMASHITA Honami Kyoto University, Research Institute for Food Science, Research Associate, 食糧科学研究所, 助手 (90252519)
TAKAHASHI Nobuyuki Kyoto University, Research Institute for Food Science, Research Associate, 食糧科学研究所, 助手 (20252520)
MIKAMI Bunzo Kyoto University, Research Institute for Food Science, Associate Professor, 食糧科学研究所, 助教授 (40135611)
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| Project Period (FY) |
1993 – 1995
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| Keywords | Food proteins / Molten globule / Food functionality / Ovalbumin / Ovotransferrin / Serum albumin |
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| Research Abstract |
The functional properties of food proteins are closely related to their conformational state. In this research project, we investigated the mechanisms for the conformational changes in food proteins, using egg white proteins (ovalbumin and ovotransferrin) and serum albumin as model proteins.
1.The X-ray crystallographic structure of both the iron-bound form of ovotransferrin was determined at 2.4 A resolution. It was found that the conformation of the protein is induced into a much more compact form by the iron-bindings.
2.The disulfide-reduced forms of ovotransferrin and serum albumin were produced by incubation with dithiothreitol and their conformational characteristics were analyzed by the circular dichroism and intrinsic tryptophan fluorescence spectra. These protein forms were found to assume the molten globule like conformation.
3.Both ovotransferrin and serum albumin were found to form opaque gels by their disulfide reduction. It was therefore concluded that the molten globule state is involved in the gelation process as crucial conformational states of these proteins.
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