| Project/Area Number |
05680055
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
家政学
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| Research Institution | Kawasaki University of Medical Welfare (1994)
Tokai Gakuen Women’s College (1993) |
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Principal Investigator |
KATO Yasuko Tokaigakuen Women's Collge professor, 臨床栄養学科, 教授 (10082356)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1994: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1993: ¥900,000 (Direct Cost: ¥900,000)
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| Keywords | Amino-carbonyl reaction / Maillard Reaction / Trypsin inhibitor / Ovomucoid / Soybean trypsin inhibitor / Borman-Birk inhibitor / Inactivation of inhibitor / Kunitzトリプシン・インヒビター / アミノ-カルボニル反応 / アミノ・カニボニル反応 |
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| Research Abstract |
The amino-carbonyl (A-C) reaction between proteins and reducing sugars proceeds in various processed and stored foods. Ovomucoid is a major component of egg white proteins, and soybean contents two major torypsin inhibitors, kuniz protease inhibitor (KSTI) and borman -birk inhibitor (BBI). They inhibits trypsin by forming a stable EI complex through their reactive sites of lysine or arginine residues.
1.The amino-carbonyl reaction of chicken and Japanese quail egg ovomucoids with glucose was investigated by keeping the powdered protein sugar mixture at 50ﾟC for a few weeks and by measuring their trypsin inhibitory activity and free amino-and guanidino-groups. The inhibitory activity of chicken ovomucoid with arginine reactive site decreased after time lag for a few days, whereas that of quail ovomucoid with lysine reactive site decreased immediately and more then 60% of the activity was lost after 5 days.
2.The A-C reaction of KSTI and BBI with glucose was investigated after the keeping as the above method. The inhibitory activity of KSTI with arginine reactive site decreased after time lag for a few days, whereas that of BBI with lysine reactive site decreased immediately and there were no inhibitory activity after 10 days. It was possible that soybean trypsin inhibitors in soybean flour was inactivated by treatment with glucose.
These inactivation profiles in ovomucoids and soybean inhibitors were in good agreement with the decrease in their free guanidino-and amino-groups, respectively.
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