Evaluating the influence of cold plasma bubbling on protein structure and allergenicity in sesame milk

Abstract

Background: Sesame is a traditional oilseed comprising essential amino acids. However, the presence of allergens in sesame is a significant problem in its consumption; thus, this study attempted to reduce these allergens in sesame oilseeds. Objective: The present study aimed to evaluate the effect of cold plasma processing on structural changes in proteins, and thereby the alteration of allergenicity in sesame milk. Method: Sesame milk (300 mL) was processed using atmospheric pressure plasma bubbling unit (dielectric barrier discharge, power: 200 V, and airflow rate: 16.6 mL/min) at different exposure times (10, 20, and 30 min). Results: The efficiency of plasma-bubbling unit as measured by electron paramagnetic resonance in terms of producing reactive hydroxyl (OH) radicals proved that generation of reactive species increased with exposure time. Further, the plasma-processed sesame milk subjected to sodium dodecyl sulfate–polyacrylamide gel electrophoresis and differential scanning calorimetery analysis revealed that plasma bubbling increased the oxidation of proteins with respect to bubbling time. The structural analysis by Fourier transform infrared spectroscopy and circular dichroism revealed that the secondary structure of proteins was altered after plasma application. This change in the protein structure helped in changing the immunoglobulin E (IgE)-binding epitopes of the protein, which in turn reduced the allergen-binding capacity by 23% at 20-min plasma bubbling as determined by the sandwich-type enzyme-linked immunosorbent assay. However, 30-min plasma bubbling intended to increase allergenicity, possibly because of increase in IgE binding due to the generation of neo epitopes. Conclusion: These changes proved that plasma bubbling is a promising technology in oxidizing protein structure, and thereby reducing the allergenicity of sesame milk. However, increase in binding at 30-min bubbling is to be studied to facilitate further reduction of the binding capacity of IgE antibodies.