超声处理对三文鱼小清蛋白构象及致敏活性的影响  

Effect of Ultrasonic Treatment on the Antigenicity and Conformation of Salmon Parvalbumin

作　　者：马涛[1] 王一侠[1] 刘艳[1] 金振涛[1] 谷瑞增[1] 鲁军[1] 

机构地区：[1]中国食品发酵工业研究院,北京市蛋白功能肽工程技术研究中心,北京100027

出　　处：《食品工业》2017年第3期160-163,共4页The Food Industry

基　　金：国家高技术研究发展计划(863计划)项目(编号:2013AA102205-02);国家十二五科技支撑项目(编号:2012BAD33B04-02);北京市科委科技创新基地培育与发展工程项目(编号:Z121106002812040);科技北京百名领军人才培养工程项目(编号:Z131110000513026)

摘　　要：小清蛋白是三文鱼中的主要过敏原蛋白组分,试验采用酶联免疫吸附试验(ELISA)、圆二色谱(CD)、ANS荧光探针及紫外可见(UV-Vis)光谱等方法,系统研究超声处理加工对三文鱼小清蛋白抗原性和结构的影响。结果表明,经超声处理后,其抗原性出现一定程度降低,且随着时间的增加其抗原性不断降低。CD色谱分析表明,经热处理后其二级结构变化不大;ANS荧光探针光谱和紫外光谱结果显示,超声处理均导致蛋白表面疏水性增加,氨基酸残基团暴露,蛋白结构改变。由此推断,三文鱼过敏原蛋白的构象改变导致了其抗原性的降低。Parvalbumin is the major allergen of salmon species. Effect of ultrasonic treatment on the antigenicity and structure of salmon parvalbumin was measured by indirect ELISA, CD, fluorescence and UV absorption spectra. The results showed that the antigenicity of parvalbumin had a slight decrease after ultrasonic treatment and the antigeicity of parvalbumin decreased with increasing time. The CD showed that the secondary structure of parvalbumin was little changed. The ANS fluorescence probe emission spectra and UV absorption spectra analysis demonstrated that the ultrasonic treatment induced an increase in surface hydrophobicity. The structure of parvalbumin was changed and amino acid residues become exposed. So the changes in the conformation of parvalbumin lead to the antigenicity degression.

关 键 词：小清蛋白 超声 构象 抗原性 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]