首页> 外文期刊>Food Chemistry >Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing
【24h】

Heat denaturation of Brazil nut allergen Ber e 1 in relation to food processing

机译:巴西坚果过敏原Ber e 1与食品加工的热变性

获取原文
获取原文并翻译 | 示例
           

摘要

Ber e 1, a major allergen from Brazil nuts, is very stable to in vitro peptic digestion. As heat-induced denaturation may affect protein digestibility, the denaturation behaviour of Ber e 1 was investigated. The denaturation temperature of Ber e 1 varies from approximately 80-110 ℃, depending on the pH. Upon heating above its denaturation temperature at pH 7.0, the protein partly forms insoluble aggregates and partly dissociates into its polypeptides, whereas heating at pH 5.0 does neither induce aggregation, nor dissociation of the protein. The denaturation temperature of approximately 110 ℃ at pH values corresponding to the general pH values of foods (pH 5-7) is very high and is expected to be even higher in Brazil nuts themselves. As a result, it is unlikely that heat processing causes the denaturation of all Ber e 1 present in food products. Consequently, the allergen is assumed to be consumed (mainly) in its native form, having a high stability towards pepsin digestion.
机译:Ber e 1是巴西坚果的主要过敏原,对体外消化消化非常稳定。由于热诱导的变性可能影响蛋白质的消化率,因此对Ber e 1的变性行为进行了研究。 Ber e 1的变性温度大约在80-110℃之间,具体取决于pH值。当在高于其7.0的变性温度下加热时,该蛋白质部分形成不溶的聚集体,并部分解离成其多肽,而在pH 5.0的加热既不诱导该蛋白质的聚集也不解离。在与食品的一般pH值(pH 5-7)相对应的pH值下,变性温度大约为110℃,预计巴西坚果本身的变性温度甚至更高。结果,加热处理不太可能引起食品中存在的所有Ber e 1变性。因此,假定过敏原主要以其天然形式消耗,对胃蛋白酶消化具有很高的稳定性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号