Abstract

The effect of linoleic acid (LA) on the IgG/IgE recognition, in vitro digestibility and immunodetection of shrimp tropomyosin (TM) was investigated. Subsequently, the simultaneous binding of LA-TM was explored using multi-spectroscopic and molecular modeling techniques. Our findings reveled that the addition of LA significantly reduced TM’s IgG/IgE immunoreactivity, digestibility, and immunodetection. Further analysis using multi-spectroscopic and molecular modeling techniques indicated that while TM’s secondary structure remained largely unchanged, its 3-D structure showed significant alterations such as increased particle size and hydrophobic surface area, and a higher number of buried hydrophobic residues exposed due to the binding of LA to TM. These structural changes rendered it difficult for target antibodies and digestive enzymes to interact with related epitopes and cleavage sites buried inside the molecule. The results obtained in this study provide valuable insights into the molecular mechanism of poor immunodetection caused by food matrix interference.

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