1999 Fiscal Year Final Research Report Summary
Structural basis for the functional properties of food Proteins
| Project/Area Number |
10460057
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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 |
HIROSE Masaaki Kyoto University, The Research Institute for Food Science, Professor, 食糧科学研究所, 教授 (60026523)
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| Co-Investigator(Kenkyū-buntansha) |
MIZUTANI Kimihiko Kyoto University, The Research Institute for Food Science, Instructor, 食糧科学研究所, 助手 (40314281)
YAMASHITA Honami Kyoto University, The Research Institute for Food Science, Instructor, 食糧科学研究所, 助手 (90252519)
TAKAHASHI Nobuyuki Kyoto University, The Research Institute for Food Science, Instructor, 食糧科学研究所, 助手 (20252520)
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| Project Period (FY) |
1998 – 1999
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| Keywords | food proteins / functional properties / ovalbumin / ovotransferrin / molecular structure |
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| Research Abstract |
Globular proteins assume different conformational states, namely the native, denatured, and molten-globule states. As model food proteins, we analyzed the mode of conformational transition of egg white ovalbumin and ovotransferrin and obtained the following results :
1. About ovalbumin : the molten-globule state was formed during the refolding from the ureadenatured state as an intermediate and also in the disulfide-reduced state at acidic pH. Recombinant ovalbumin produced in E coli was found to assume essentially the same conformation as egg white ovalbumin but to lack the post-translational modification. According to the observation that the recombinant protein underwent the alkaline-dependent thermostabilization, the post-translational modification was not involved in the thermostabilization mechanism. An ovalbumin variant R339T was found to be transformed into a thermostabilized form following the cleavage at the P1-P1'site.
2. About ovotransferrin : As a structural basis for the structural transition, crystal structure of the apo from of ovotransferrin was determined. Decreased formability of egg white following heat treatments was found to be due to the denaturation of ovotransferrin that can be minimized by addition of some anions.
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