Effect of tyrosinase-aided crosslinking on the IgE binding potential and conformational structure of shrimp (Metapenaeus ensis) tropomyosin. (15th May 2018)

• Record Type: Journal Article
• Authors: Ahmed, Ishfaq; Lv, Liangtao; Lin, Hong; Li, Zhenxing; Ma, Jiaju; Guanzhi, Chen; Sun, Lirui; Xu, Lili
• Is Part Of: Food chemistry. Volume 248(2018)
• Page Start: 287
• Page End: 295
• Publication Date: 2018-05-15
• Subjects: Shrimp tropomyosin -- Tyrosinase -- Caffeic acid -- Cross-linking -- IgE-binding -- Protein structure; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2017.12.071
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Treatment of shrimp TM with Tyr and CA led to the formation of crosslinks. Crosslinking and oxidation altered the structure and the IgG/IgE binding levels. Tyr and CA showed effective in mitigating allergenicity caused by shrimp TM. Hypoallergenic food could possibly be tailored via Tyr-catalyzed crosslinking. Abstract: The present study was performed to determine crosslinking and oxidative reactions catalyzed by tyrosinase (Tyr), caffeic acid (CA) and their combination with respect to IgE binding potential and conformational structure of shrimp tropomyosin (TM) . Cross-links and IgE binding potentials were analyzed by SDS-PAGE, western blot and indirect ELISA. While structural changes were characterized using surface hydrophobicity, ultraviolet (UV), fluorescence and circular dichroism (CD) spectroscopies. Maximum reduction in the IgG (37.19%) and IgE binding potentials (49.41%) were observed when treated with 2000 nkat/g Tyr + CA, as indicated by ELISA analyses. These findings correlated well with the denaturation of protein, as evident by slight blue shift and alterations in the ellipticities observed via structural analyses. The results demonstrated that addition of CA mediator with Tyr pronouncedly enhanced crosslinking, and altered the conformational structure, thereby mitigated allergenicity of TM, thus showing promise in developing novel food structures with reduced allergenic potential.