Shrimp is popular for its delicious flavor and high nutritional value. However, The allergenic proteins in shrimp is also one of main “Eight allergens” [1]. Shrimp allergy often cause respiratory, urticaria, rhinitis, anaphylactic shock, and can even be life-threatening [2].

Shrimp tropomyosin (TM) is the main allergen with ∼36 kDa molecular weight. To control the risk of food allergies, different processing methods were performed to reduce the allergenicity of TM, such as irradiation, ultrasound, high-pressure processing (HPP) and so on. The IgE binding ability of shrimp TM can be significantly reduced after 10 kGy electron beam (EB) radiation [3]. Huang et al. reported that the allergenicity of shrimp TM can be reduced by 30 Hz and 800 W high intensity ultrasound. Faisal et al. [4] found that the allergenicity of shrimp TM can be reduced by 600 MPa HPP. Although these studies provide the necessary technical support to reduce the allergenicity of shrimp TM, the original quality and morphology of the shrimp was easily destroyed.

Compared to traditional processing methods, glycosylation often was a promising method for reducing the allergenicity of food allergens. Galactosamine (D) is a widely used primary amine sugar [[5], [6], [7]]. The allergenicity of shrimp TM was weaken after glycosylation modification [8]. The food allergy induced by Shrimp TM can be alleviated through glycosylation, which significantly reduces the allergenicity and alleviates the allergic symptoms. [9]. These studies were considered to offer the necessary support for controlling the risk of shrimp allergy. However, glycosylation reaction is complex, even form harmful glycosylation end products [10]. The enzymatic catalyzed glycosylation enables the specific glycosylation modification of amino acid residues on food allergens [11]. Especially modify the allergenic epitopes in order to effectively achieve targeted reduction of allergen allergenicity. In addition, by analyzing the changes in the molecular structure and allergenicity of allergens after TGcG, it is possible to build up an information base on the changes in the structure and allergenicity of allergens. In our previous study, the IgE binding ability of sword shrimp TM were analyzed by transglutaminase (TG)-catalyzed glycosylation [12,13]. However, the digestive stability and allergenicity by mouse model have not been studied in depth.

The study aimed to investigate the digestive stability and allergenicity of shrimp TM by TGcG. The structure of TGcG-TM was determined by SDS-PAGE, intrinsic fluorescence and CD analysis. Importantly, the digestive stability was analyzed by simulated gastrointestinal fluid. In addition, the allergenicity of TGcG-TM were analyzed through the mouse model. This study will provide detailed technical support for developing new hypoallergenic foods.