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浙江大学学报（农业与生命科学版）
浙江大学学报(农业与生命科学版)  2013, Vol. 39 Issue (6): 679-686    DOI: 10.3785/j.issn.1008-9209.2013.01.082
食品科学     
大菱鲆过敏原氧化后理化性质及与IgE结合能力的变化
陆宗超， 李振兴*， 张立敏， 林洪
（中国海洋大学食品安全实验室，山东 青岛 266003）
Physicochemical properties and IgE binding ability changes of turbot allergen during oxidation
LU Zongchao, LI Zhenxing*, ZHANG Limin, LIN Hong
(Seafood Safety Laboratory, Ocean University of China, Qingdao, Shandong 266003, China)
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摘要： 为了探明在蛋白质氧化过程中过敏原理化性质的变化规律，以大菱鲆为研究对象，采用羟基自由基氧化体系对大菱鲆过敏原进行不同程度的氧化，检测其功能基团的变化规律，并分别利用鱼类过敏患者血清和兔抗大菱鲆小清蛋白多克隆抗体分析大菱鲆过敏原小清蛋白免疫功能的变化规律.结果表明：大菱鲆蛋白经过5 h氧化后有27%的蛋白质发生了沉淀；氧化5 h后在上清液和沉淀中的蛋白质羰基含量分别增加了9.7倍和2.0倍，巯基含量分别降低了13.5%和29.1%.与对照组相比，实验组12、26和41 ku处的蛋白质含量减少，然而在沉淀中36 ku左右处的蛋白质含量随着氧化时间的增长而增加.免疫印迹结果显示，实验组蛋白与鱼类过敏患者血清之间的特异性反应强度降低.间接酶联免疫结果表明，经过5 h氧化处理后在上清液和沉淀中大菱鲆过敏原活性分别降低了16.7%和31.5%.说明氧化改变了大菱鲆蛋白的理化性质，并可能改变了大菱鲆蛋白的结构，进而影响大菱鲆过敏原蛋白的功能性质.
Abstract: During food processing and storage, proteins are susceptible to the action of any hydroxyl radicals. Reactive oxygen species (ROS) are naturally generated in food systems. Oxidative processes in food result in decreased quality by causing changes in color, texture, flavor and nutritional value. Currently, many researchers have reported that the proteins are the primary target of oxidizing radicals in vivo. Protein solubility and functional activity reduction were revealed in meat proteins due to simulation oxidation system inducing polymerization and degradation. Furthermore, the effects of metalcatalyzed oxidation systems in fish proteins were also reported. To date, there is no correlation study between protein oxidation and fish allergen. Therefore, the objective of this study was to explore modification of fish muscle proteins by oxidizing radicals, including functional properties such as the allergenicity and functionality groups. To investigate the effects of protein oxidation on the content of carbonyl and sulfhydryl, turbot proteins (allergens) were exposed to a free radical generating system and incubated at 37 ℃ for different intervals. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDSPAGE) was used to analyze the alterations of turbot proteins. The alterations of the parvalbumin allergenicity were investigated by Western blot with sera from three fish allergic patients and by indirect enzymelinked immunosorbent assay (ELISA) method with rabbit antiturbot parvalbumin polyclonal antibody. The results showed that 27% proteins were precipitated when exposed to the hydroxyl radical oxidation systems for 5 h. The contents of carbonyl groups in supernatant and precipitate increased by 9.7 and 2.0 times after 5 h oxidation, and sulfhydryl groups decreased by 13.5% and 29.1%, respectively. The electrophoretic patterns of control showed that the contents of 12, 26 and 41 ku proteins extremely decreased. However, the contents of 36 ku proteins increased with increasing oxidative time, which suggests that the aggregates might be formed via noncovalent interactions. IgE Western blot indicated that immunogenicity of proteins decreased with increasing oxidation time. Furthermore, indirect ELISA indicated that the immunogenicity of parvalbumin in both supernatant and precipitate decreased by 16.7% and 31.5% after 5 h oxidation, respectively. It is concluded that the oxidation alters the physicochemical properties of turbot proteins (allergens) and this may lead to the modifications of chemical structure and functionalities of the proteins. The chemical changes occur concomitantly with protein functionalities. However, oxidative damage can also cause important loss of quality. This research could help fish researchers and processors to develop strategies to minimize the oxidation reactions in fish foods during storage and processing.
出版日期: 2013-11-20
CLC:  TS 254  
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陆宗超
李振兴*
张立敏
林洪

引用本文:

陆宗超， 李振兴*， 张立敏， 林洪. 大菱鲆过敏原氧化后理化性质及与IgE结合能力的变化[J]. 浙江大学学报(农业与生命科学版), 2013, 39(6): 679-686.

LU Zongchao, LI Zhenxing*, ZHANG Limin, LIN Hong. Physicochemical properties and IgE binding ability changes of turbot allergen during oxidation. Journal of Zhejiang University (Agriculture and Life Sciences), 2013, 39(6): 679-686.

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http://www.zjujournals.com/agr/CN/10.3785/j.issn.1008-9209.2013.01.082    或    http://www.zjujournals.com/agr/CN/Y2013/V39/I6/679

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