Mechanism of Cold Plasma Combined with Glycation in Altering IgE-Binding Capacity and Digestion Stability of Tropomyosin from Shrimp.

Abstract

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 (Penaeus chinensis). 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 (D137 and E218) and occupied the potential glycation sites, leading to sequent glycation on conserved areas of TM, especially the epitope L130-Q147. 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 K5, K6, K30, and R133, 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.