Abstract
Tropomyosin (TM) is a heat-stable protein that plays a crucial role as a major pan-allergen in crustacean shellfish. Despite the high thermal stability of the TM structure, its IgG/IgE binding ability, immunodetection, and in vitro digestibility can be negatively influenced by glycation during food processing, and the underlying mechanism remains unclear. In this study, TM was subjected to glycosylation using various sugars and temperatures. The resulting effects on IgG/IgE-binding capacity, immunodetection, and in vitro digestibility were analyzed, meanwhile, the structural alterations and modifications using spectroscopic and LC-MS/MS analysis were determined. Obtained results suggested that the IgG/IgE binding capacity of glycosylated TM, immunodetection recovery, and in vitro digestibility were significantly reduced depending on the degree of glycosylation, with the greatest reduction occurring in Rib-TM. These changes may be attributable to structural alterations and modifications that occur during glycosylation processing, which could mask or shield antigenic epitopes of TM (E3: 61-81, E5b: 142-162, and E5c: 157-183), subsequently reducing the immunodetection recognition and digestive enzyme degradation. Overall, these findings shed light on the detrimental impact of glycation on TMs potential allergenicity and digestibility immunodetection and provide insights into the structural changes and modifications induced by thermal processing.