Abstract
The study aimed to investigate the digestive stability and allergenicity of shrimp tropomyosin (TM) by transglutaminase (TG)-catalyzed glycosylation (TGcG). The structure of samples was analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), circular dichroism (CD), fluorescence, and surface hydrophobicity. The digestive stability was determined by simulated gastrointestinal fluid. The allergenicity was evaluated by in mice model. The results demonstrated that TGcG induced structural alterations in TM. The TGcG method enhanced the anti-digestive ability of TM. Compared to native TM, TGcG-treated TM showed significantly reduced allergenicity, evidenced by 30 % lower histamine and 23 % decreased mMCP-1 levels in serum. Mast cell activation markers (c-Kit+/FcεRI+) were downregulated by 64 %, and duodenal tissue damage was reduced by 45 %. These effects correlated with improved Th1/Th2 Immune balance. The findings highlight TGcG as an effective strategy to mitigate TM allergenicity while preserving protein functionality, offering practical potential for developing hypoallergenic seafood products.