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.
J Agric Food Chem. 2023 Oct 25;71(42):15796-15808. doi: 10.1021/acs.jafc.3c04796. Epub 2023 Oct 10.
Tropomyosin (TM) is a major crustacean allergen, and the present studies have tried to reduce its allergenicity by processing technologies. However, most research stopped on the allergenicity and structure of allergens, while information about epitopes was less. In this study, we first investigated the effects of cold plasma (CP) combined with glycation (CP-G) treatment on the processing and trypsin cleavage sites of TM from shrimp (). The results showed a significant reduction in the IgE-binding capacity of TM after CP-G treatment, with a maximum reduction of 30%. This reduction was associated with the combined effects: modification induced by CP destroyed the core helical structure (D and E) and occupied the potential glycation sites, leading to sequent glycation on conserved areas of TM, especially the epitope L-Q. Additionally, CP-G treatment decreased the digestion stability of TM by increasing the number of cleavage sites of trypsin and improving the efficiency of some sites, including K, K, K, and R, resulting in a lower IgE-binding capacity of digestion products, which fell to a maximum of 20%. Thus, CP-G is a valuable and reliable processing technology for the desensitization of aquatic products.
原肌球蛋白（TM）是一种主要的甲壳类过敏原，目前的研究试图通过加工技术来降低其致敏性。然而，大多数研究都停留在过敏原的致敏性和结构上，而关于表位的信息较少。在这项研究中，我们首先研究了冷等离子体（CP）与糖化（CP-G）联合处理对虾 TM 的加工和胰蛋白酶切割位点的影响。结果表明，CP-G 处理后 TM 的 IgE 结合能力显著降低，最大降低 30%。这种降低与以下联合作用有关：CP 诱导的修饰破坏了核心螺旋结构（D 和 E）并占据了潜在的糖化位点，导致 TM 保守区域的连续糖化，特别是表位 L-Q。此外，CP-G 处理通过增加胰蛋白酶的切割位点数量和提高某些位点的效率（包括 K、K、K 和 R）来降低 TM 的消化稳定性，导致消化产物的 IgE 结合能力降低，最大降低幅度达到 20%。因此，CP-G 是一种有价值且可靠的水产品脱敏加工技术。
