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作 者:熊子奕 谭宏凯 胡永芯 武涌[1,3] 陈红兵 李欣[1,2] XIONG Ziyi;TAN Hongkai;HU Yongxin;WU Yong;CHEN Hongbing;LI Xin(State Key Laboratory of Food Science and Technology,Nanchang University,Nanchang 330047,China;College of Food Science and Technology,Nanchang University,Nanchang 330047,China;Jiangxi Provincial Key Laboratory of Interdisciplinary Science,Nanchang University,Nanchang 330047,China;Sino-German Joint Research Institute,Nanchang University,Nanchang 330047,China)
机构地区:[1]南昌大学食品科学与技术国家重点实验室,江西南昌330047 [2]南昌大学食品学院,江西南昌330047 [3]南昌大学高等研究院微纳米科学与技术省重点实验室,江西南昌330047 [4]南昌大学中德联合研究院,江西南昌330047
出 处:《食品科学》2022年第16期73-80,共8页Food Science
基 金:“十三五”国家重点研发计划重点专项(2018YFC1604205);南昌大学食品科学与技术国家重点实验室目标导向课题(SKLF-ZZA-201912)。
摘 要:以牛乳乳清蛋白为研究对象,探究臭氧处理对乳清蛋白的结构及致敏性的影响。分别测定臭氧处理0、5、10、15、20 s和25 s后乳清蛋白氨基酸组分、巯基和二硫键含量的变化,并采用圆二色光谱仪、紫外分光光度计和荧光分光光度计等光谱学技术分析其结构变化,最后利用间接竞争酶联免疫吸附剂测定(enzyme linked immunosorbentassay,ELISA)分析体外特异性抗体的结合能力变化,用于评估潜在的致敏性。结果表明,臭氧处理会使乳清蛋白中部分氨基酸的含量降低,游离巯基含量由5.78μmol/g减少至2.13μmol/g,总巯基含量由14.98μmol/g减少至12.97μmol/g,二硫键含量则由4.60μmol/g升高至5.42μmol/g。光谱学分析表明,臭氧处理后乳清蛋白的二级结构改变、三级结构变得松散,但随着处理时间的延长,部分蛋白分子之间相互聚集,二硫键的增加也使乳清蛋白的空间结构重归有序。间接竞争ELISA的结果表明臭氧处理后乳清蛋白的致敏性明显下降。综上所述,臭氧处理在降低乳清蛋白致敏性、提高乳蛋白食品安全性上具有良好的研究潜力和开发前景。In this study,we explored the effect of ozone treatment on the structure and allergenicity of milk whey protein.The changes in amino acid composition,sulfhydryl group and disulfide bond contents of whey protein were measured after ozone treatment for 0,5,10,15,20 and 25 s.Circular dichroism spectroscopy,ultraviolet spectroscopy and fluorescence spectroscopy were applied for analyzing the structural changes.Finally,the ability to bind to specific antibodies in vitro was determined by indirect competitive enzyme-linked immunosorbent assay(ic-ELISA)to evaluate the potential allergenicity.The results showed that ozone treatment reduced the contents of some amino acids in whey protein.It reduced the contents of free sulfhydryl and total sulfhydryl groups from 5.78 to 2.13μmol/g and from 14.98 to 12.97μmol/g,respectively,but increased the content of disulfide bonds from 4.60 to 5.42μmol/g.Spectroscopic analysis showed that the secondary structure of whey protein was changed.At the early stage of ozone treatment,the tertiary structure became loose,but as the treatment time increased,some protein molecules gathered together and the content of disulfide bonds increased,causing the spatial structure of whey protein to return to its original ordered state.The results of ic-LISA showed that the allergenicity of whey protein decreased significantly after ozone treatment.In conclusion,ozone treatment holds great potential in improving the safety of milk-containing foods.
分 类 号:TS252.1[轻工技术与工程—农产品加工及贮藏工程]
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