Inactivation of trypsin inhibitors in foods by amino-carbonyl reaction

通过氨基-羰基反应灭活食品中的胰蛋白酶抑制剂

• 批准号: 05680055
• 负责人: KATO Yasuko
• 金额: $ 1.02万
• 依托单位: Kawasaki University of Medical Welfare (1994)Tokai Gakuen Women’s College (1993)
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (C)
• 财政年份: 1993
• 资助国家: 日本
• 起止时间: 1993 至 1994
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-05680055/
• 关键词: 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

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.

蛋白质和还原糖之间的氨基-羰基(A-C)反应在各种加工和储存的食品中进行。类卵粘蛋白是蛋清蛋白的主要成分，大豆中含有两种主要的胰蛋白酶抑制剂，即Kuniz蛋白水解酶抑制剂(KSTI)和Borman-Birk抑制剂(BBI)。它们通过其赖氨酸或精氨酸残基形成稳定的EI复合体来抑制胰酶。1.通过将蛋白糖粉混合物在50ﾟC下放置几周，并通过测定它们的胰酶抑制活性和游离氨基和胍基，研究了鸡蛋卵粘蛋白与葡萄糖的氨基-羰基反应。鸡类卵粘蛋白具有精氨酸反应部位的抑制活性在几天后下降，而鹌鹑类卵粘蛋白具有赖氨酸反应部位的抑制活性立即下降，5天后失去60%以上的活性。2.采用上述方法研究了KSTI和BBI与葡萄糖的A-C反应。含精氨酸反应部位的KSTI的抑制活性在几天后下降，而含有赖氨酸反应部位的BBI在10d后立即下降，没有抑制活性。大豆粉中的大豆胰酶抑制剂可能通过葡萄糖处理而失活，卵粘蛋白和大豆抑制剂中的这些失活曲线分别与其游离基和氨基的减少相一致。

项目成果

加藤保子: "保育園児の食事性アレルギーの実態と母子の食歴" 川崎医療福祉学会誌. 4. 145-152 (1994)

加藤泰子：“保育园儿童饮食过敏的实际状况以及母亲和儿童的饮食史”川崎健康福利学会杂志 4. 145-152 (1994)。

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).

Yasuko Kato 和 Tsukasa Matsuda：“鸡和鹌鹑卵类粘蛋白的糖化：通过阻断反应位点的精氨酸和赖氨酸残基导致胰蛋白酶抑制活性失活”J. Agric。

Y.Kato,T.Aoki,N.kato,R.Nakamura,T.Hatsuda: "Modification of Ovalbumin with glucose-b-phosphate.by Amino-Carbonyl Reaction -Improvement of protein Heat Stabilit and Erulsifying Actrity." J.Agric Food Dhem.43. 301-305 (1995)

Y.Kato、T.Aoki、N.kato、R.Nakamura、T.Hatsuda：“用葡萄糖-b-磷酸修饰卵清蛋白。通过氨基-羰基反应 - 改善蛋白质的热稳定性和乳化活性。”

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).

Yasuko Kato 和 Tsukasa Matsuda：“鸡和鹌鹑卵类粘蛋白的糖化：通过阻断其反应位点的精氨酸和赖氨酸残基来失活胰蛋白酶抑制活性”J.Agric.Food Chem。

T.Aoki,T,Fukumoto,T,Kimura.Y.Kato,T,Matsuda: "Whey Protein-and Egg White Protein-Glucose 6-Phoshate Conjugates wite Calcium phosphate-aolubiliginz Properties." Biosci Biotech.Biochem.,. 58. 1727-1728 (1994)

T.Aoki,T,Fukumoto,T,Kimura.Y.Kato,T,Matsuda：“乳清蛋白-和蛋清蛋白-葡萄糖 6-磷酸盐缀合物，具有磷酸钙-aolubiliginz 特性。”