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1994 Fiscal Year Final Research Report Summary

Inactivation of trypsin inhibitors in foods by amino-carbonyl reaction

Research Project

Project/Area Number 05680055
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 家政学
Research InstitutionKawasaki University of Medical Welfare (1994)
Tokai Gakuen Women’s College (1993)

Principal Investigator

KATO Yasuko  Tokaigakuen Women's Collge professor, 臨床栄養学科, 教授 (10082356)

Project Period (FY) 1993 – 1994
KeywordsAmino-carbonyl reaction / Maillard Reaction / Trypsin inhibitor / Ovomucoid / Soybean trypsin inhibitor / Borman-Birk inhibitor / Inactivation of inhibitor
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.

  • Research Products

    (2 results)

All Other

All Publications (2 results)

  • [Publications] Yasuko Kato and Tsukasa Matsuda: "Glycation of chicken and quail ovomucoids: Inactivation loss in trypsin inhibitory activity by the blocking of arginine and lysine residues at their reactive sites" J. Agric. Food Chem. (Submitted).

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Yasuko Kato and Tsukasa Matsuda: "Glycation of chicken and quail ovomucoids : Inactivation loss in trypsin inhibitory activity by the blocking of arginine and lysine residues at their reactive sites" J.Agric.Food Chem. (Submitted).

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1996-04-15  

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