Evidence of regained antigenic activity during proteinase treatment in hydrolyzate of denatured insoluble allergen in processed foods

加工食品中变性不溶性过敏原水解产物在蛋白酶处理过程中恢复抗原活性的证据

• 批准号: 10680155
• 负责人: KATO Yasuko
• 金额: $ 1.92万
• 依托单位: Kawasaki University of Medical Welfare
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 1998
• 资助国家: 日本
• 起止时间: 1998 至 1999
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-10680155/
• 关键词: allergen; trypsin; pepsin; chymotrypsin; egg white; ovomucoid; hydrolyzate; wheat flour processed foods; スキムミルク; β-ラクトグロブリン; 不溶化; 鶏卵; ペプシン消化

Ovomucoid, one of the major egg white allergens, changed in denatured insoluble and the antigenic activity was disappeared in the processes of bread or pasta making. It is the most necessary for application of oral challenge of the products as the next step study that the hydrolyzate of the insoluble ovomucoid in the products dose not gain the antigenic activity. Insoluble egg allergenic protein in the wheat-flour egg white complex is in vitro hydrolyzed by pepsin, trypsin and chymotrypsin. The aim of this study that allergenic patients for egg are possible to eat bread and pasta supplemented egg.1. Antigenic activities of the hydrolyzate of egg white proteins, ovomucoid and ovalbumin (OVA), in simulated gastric fluid were analyzed with ELISA competitive inhibition using rabbit anti OM or OVA serum. Heated OM was considerably more resistant to pepsin hydrolysis than was heated OVA. OM antigenic activity in heated egg white decreased more remarkably than that of heated OM. The OM antigenic activities in both supernatant and precipitate separated from pepsin digests of bread and dough samples supplemented with egg white were examined with ELISA competitive inhibition and immunoblotting analysis. OM antigenic activity in both supernatant and precipitate of bread hydrolyzed by pepsin for 120 min disappeared completely, though it remained in both hydrolyze of dough. 3. OM antigenic activity in pasta dough and boiled pasta supplemented with egg white were also disappeared in pepsin digests of boiled pasta but in those of dough.

蛋清的主要过敏原之一卵黏液样蛋白在面包和面食加工过程中变性不溶性发生变化，抗原活性消失。研究产品中不溶性卵黏液的水解产物是否具有抗原性，是今后产品口服激发应用的关键。小麦-面粉蛋白复合物中的不溶性鸡蛋致敏蛋白被胃蛋白酶、胰蛋白酶和凝乳胰蛋白酶体外水解。本研究的目的是使对鸡蛋过敏的患者可以食用面包和面食补充鸡蛋。采用ELISA法对兔抗OM或OVA血清对模拟胃液中蛋清蛋白、卵黏液和卵清蛋白（OVA）水解产物的抗原活性进行了分析。加热后的OM比加热后的OVA更能抵抗胃蛋白酶的水解。加热后蛋清的OM抗原活性比加热后的OM降低得更明显。采用ELISA竞争抑制法和免疫印迹法检测添加蛋清的面包和面团胃蛋白酶消化液分离的上清液和沉淀的OM抗原活性。面包经胃蛋白酶水解120 min后的上清液和沉淀物中OM抗原活性完全消失，而面团水解后的上清液和沉淀物中OM抗原活性仍然存在。3. 面食的OM抗原活性在面食的胃蛋白酶消化酶中消失，而在面食的胃蛋白酶消化酶中消失。

项目成果

小澤慶子 ら: "低アレルゲン化卵料理の調製"New Food Industry. 41. 63-70 (1999)

Keiko Ozawa 等人：“低过敏性鸡蛋菜肴的制备”《新食品工业》41. 63-70 (1999)。

T. Aoki et al.: "Improvement of heat stability and emulsfying activity of Ovalbumin by conjugation with glucuronic acid through the Mailard rection"Food Research International. 32. 129-133 (1999)

T. Aoki 等人：“通过美拉德反应与葡萄糖醛酸结合，改善卵清蛋白的热稳定性和乳化活性”国际食品研究。

Yasuko Kato et al.: "Ovomucoid Rendered Insoluble by Heating with Wheat Gluten but not with Milk Casein"Biosci.Biotechnol.Biochem.. 64・1. 198-201 (2000)

Yasuko Kato 等人：“卵粘蛋白通过与小麦面筋加热而不与牛奶酪蛋白混合而变得不溶”Biosci.Biotechnol.Biochem.. 64・1 (2000)。

小澤慶子,加藤保子 他: "加熱オボムコイド除去卵の調製法とアレルギー患者血清を用いたアレルゲン活性の評価"日本栄養・食糧学会誌. 53・2(in press). (2000)

Keiko Ozawa、Yasuko Kato 等人：“加热的无卵类粘蛋白鸡蛋的制备和使用过敏患者血清评估过敏原活性”，日本营养与食品科学学会杂志 53, 2（出版中）。

Yasuko Kato et al.: "Ovomucoid Rendered Insoluble by Heating with Wheat Gluten but not with Milk Ca*ein"Biosci. Biotechuol. Biochem.. 64. 198-201 (2000)

Yasuko Kato 等人：“卵类粘蛋白通过与小麦面筋加热而不是与牛奶钙蛋白一起加热而变得不溶”Biosci。