Cheng Jun-Hu, Wang Huifen, Sun Da-Wen
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Academy of Contemporary Food Engineering, South China University of Technology, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China; Engineering and Technological Research Centre of Guangdong Province on Intelligent Sensing and Process Control of Cold Chain Foods, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China.
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Academy of Contemporary Food Engineering, South China University of Technology, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China; Engineering and Technological Research Centre of Guangdong Province on Intelligent Sensing and Process Control of Cold Chain Foods, Guangzhou Higher Education Mega Centre, Guangzhou 510006, China; Food Refrigeration and Computerized Food Technology (FRCFT), Agriculture and Food Science Centre, University College Dublin, National University of Ireland, Belfield, Dublin 4, Ireland.
Int J Biol Macromol. 2023 Apr 15;234:123690. doi: 10.1016/j.ijbiomac.2023.123690. Epub 2023 Feb 17.
Tropomyosin (TM) is a major allergen in crustaceans, and its allergenicity mainly depends on epitopes. In this study, the locations of IgE-binding sites between plasma active particles and allergenic peptides of TM in shrimp (Penaeus chinensis) during cold plasma (CP) treatment were explored. Results showed that the IgE-binding ability of two critical peptides (P1 and P2) increased and then decreased by 9.97 % and 19.50 % after 15 min of CP treatment. It was the first time to show that the contribution rate of target active particles was •O > e > •OH for reducing IgE-binding ability by 23.51 %-45.40 %, and the contribution rates of other long-lived particles including NO and NO was about 54.60 %-76.49 %. In addition, Glu131 and Arg133 in P1 and Arg255 in P2 were certified as the IgE sites. These results were helpful for accurately controlling TM allergenicity, shedding more light on allergenicity mitigation during food processing.
原肌球蛋白（TM）是甲壳类动物中的主要过敏原，其致敏性主要取决于表位。本研究探讨了在冷等离子体（CP）处理过程中，虾（中国对虾）血浆活性粒子与TM致敏肽之间IgE结合位点的位置。结果表明，两种关键肽（P1和P2）的IgE结合能力在CP处理15分钟后先升高后降低，分别降低了9.97%和19.50%。首次表明，目标活性粒子降低IgE结合能力的贡献率为•O > e > •OH，降低幅度为23.51% - 45.40%，其他包括NO和NO₂在内的长寿命粒子的贡献率约为54.60% - 76.49%。此外，P1中的Glu131和Arg133以及P2中的Arg255被确认为IgE位点。这些结果有助于准确控制TM的致敏性，为食品加工过程中的致敏性减轻提供更多启示。
