Comparison of digestibility and potential allergenicity of raw shrimp (Litopenaeus vannamei) extracts in static and dynamic digestion systems

• Published in: Food chemistry Vol. 345; p. 128831
• Main Authors: Guo, Yuman, Luo, Chen, Xu, Lili, Lin, Hong, Li, Zhenxing, Pavase, Tushar Ramesh, Wu, Yeting, Chen, Yan
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 30.05.2021
• Subjects: Allergens - immunology; Animals; Digestibility; Digestion; Dynamic digestion system; Food Hypersensitivity - immunology; Humans; Immunoglobulin E - chemistry; Immunoglobulin E - immunology; Molecular Weight; Penaeidae - immunology; Potential allergenicity; Seafood - analysis; Shrimp proteins; Static digestion system; Tropomyosin - immunology; Static digestion system; Dynamic digestion system; Shrimp proteins; Digestibility; Potential allergenicity
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2020.128831

•The dynamic system simulated ingestion, secretion, pH curve, and GI emptying.•RSE proteins showed different hydrolysis behaviors in the two systems.•TM revealed better digestion stability in the dynamic system.•Good approximation of Mw of IgG/IgE binding fragments in the two systems.•Dynamic conditions affected the histamine release trend during digestion. In this work, a simplified dynamic digestion system was developed, and used for comparing the digestibility and potential allergenicity of raw shrimp extracts (RSE) in static and dynamic digestion systems. Protein hydrolysis was analyzed by electrophoresis, and the potential allergenicity was reflected in IgG/IgE binding ability and activation of basophils. In comparison with static digestion, protein hydrolysis indicated different kinetic behaviors, especially tropomyosin (TM) showed better digestion stability during dynamic digestion. The potential allergenicity of RSE exhibited different changing trends with digestion in the two systems. However, the apparent molecular weight (Mw) of immune fragments (>11 kDa) showed good approximation, and the IgE-binding fragment near 70 kDa revealed outstanding digestion stability than primordial protein in both systems. In conclusion, the dynamic conditions had a significant impact on the assessment of the persistence and potential allergenicity of digestion-resistant allergens, while the apparent Mw of IgG/IgE binding hydrolysate was not affected.