Changing the IgE Binding Capacity of Tropomyosin in Shrimp through Structural Modification Induced by Cold Plasma and Glycation Treatment

Abstract

Tropomyosin (TM) is the major allergen of shrimp (Penaeus chinensis). Previous studies showed that separate cold plasma or glycation have their drawback in reducing allergenicity of TM, including effectiveness and reliability. In the current study, a new processing combining cold plasma (CP) and glycation was proposed and its effect on changing IgE binding capacity of TM from shrimp was investigated. Obtained results showed the IgE binding capacity of TM was reduced by up to 40% after CP (dielectric barrier discharge, 60 kV, 1.0 A) combined with glycation treatment (4 h, 80 °C), compared with the less than 5% reduction after single CP or glycation treatment. Notably, in contrast to the general way of CP prompting glycation, this study devised a new mode of glycation with ribose after CP pretreatment. The structural changes of TM were explored to explain the decreased IgE binding reactivity. The results of multi-spectroscopies showed that the secondary and tertiary structures of TM were further destroyed after combined treatment, including the transformation of 50% α-helix to β-sheet and random coils, the modification and exposure of aromatic amino acids, and the increase of surface hydrophobicity. The morphology analysis using atomic force microscope revealed that the combined processing made the distribution of TM particles tend to disperse circularly, while it would aggregate after either processing treatment alone. These findings confirmed the unfolding and reaggregation of TM during combined processing treatment, which may result in the remarkable reduction of IgE binding ability. Therefore, the processing of CP pretreatment combined with glycation has the potential to reduce or even eliminate the allergenicity of seafood.