Evaluation of IgE binding, to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis) and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit

Evaluation of IgE binding, to proteins of hardy (Actinidia arguta), gold (Actinidia chinensis) and green (Actinidia deliciosa) kiwifruits and processed hardy kiwifruit concentrate, using sera of individuals with food allergies to green kiwifruit
复制标题

DOI:
10.1016/j.fct.2006.01.005
复制
发表时间:
2006-07-01
影响因子:
4.3
通讯作者:
Goodman, Richard E.
Goodman, Richard E.
中科院分区:
农林科学2区
文献类型:
--
作者:
Chen, Lingyun;Lucas, Jane S.;Goodman, Richard E.

文献摘要

被引文献

相似文献

背景:自从绿色猕猴桃在30年前被引入北美和欧洲以来,对它的过敏已经变得很普遍。金猕猴桃,最近才被商业化,已经被证明可以结合一些对绿猕猴桃过敏的人的IgE。耐寒猕猴桃是目前在北美种植的第三种水果,具有作为新鲜水果和加工食品的潜在应用价值。目的:比较耐寒猕猴桃提取物和加工猕猴桃浓缩液中蛋白质的IgE结合特性,以及与绿猕猴桃和金猕猴桃提取物的IgE结合特性,以评价过敏交叉反应的可能性。方法:采用免疫印迹法和直接酶联免疫吸附法(ELISA)检测对猕猴桃过敏者和非过敏者血清中绿猕猴桃、金猕猴桃和耐热猕猴桃热浓缩物中可溶性蛋白的IgE结合。结果:鉴定出特异性耐寒猕猴桃蛋白的标记IgE结合。然而,热加工猕猴桃浓缩液的IgE结合量明显低于生猕猴桃提取物。结论:这些结果表明,一些对猕猴桃过敏的人在食用生猕猴桃时可能会出现过敏交叉反应。然而,耐热猕猴桃的热处理改变了致敏蛋白结构,显著降低了体外IgE结合。加工猕猴桃可能会降低那些对生猕猴桃过敏的人引起过敏反应的风险。(c) 2006 Elsevier Ltd.版权所有。
Background: Allergy to green kiwifruit has become common since the fruit was introduced in North America and Europe 30 years ago. Gold kiwifruit, more recently introduced commercially, has been shown to bind IgE from some individuals allergic to green kiwifruit. Hardy kiwifruit is a third species that is now cultivated in North America with potential application as a fresh fruit and in processed foods.Objective: To compare the IgE binding properties of proteins in hardy kiwifruit extract and processed hardy kiwifruit concentrate to each other and to extracts of green and gold kiwifruits to evaluate the potential for allergic cross-reactions.Methods: Sera from kiwifruit-allergic subjects and individuals without allergies to kiwifruit were assayed for IgE binding to soluble proteins in green, gold and hardy kiwifruits and heat-processed concentrate from hardy kiwifruit using immunoblots and direct enzymelinked immunosorbent assay (ELISA).Results: Marked IgE binding to specific hardy kiwifruit proteins was identified. However, IgE binding to heat-processed hardy kiwifruit concentrate was remarkably lower than to the raw fruit extract.Conclusions: These results suggest that some kiwifruit-allergic individuals may suffer allergic cross-reactions if they consume raw hardy kiwifruit. However, heat processing of the hardy kiwifruit alters allergenic protein structure, dramatically reducing in vitro IgE binding. Processing likely reduces the risk of eliciting an allergic response in those with allergies to raw kiwifruit. (c) 2006 Elsevier Ltd. All rights reserved.