Effects of Interaction on the Structure and Potential Allergenicity of Ovalbumin and Lysozyme

doi:10.7506/spkx1002-6630-20190124-307

Abstract

Abstract: To understand the effect of protein-protein interactions during heat treatment on the structure and allergenicity of ovalbumin (OVA) and lysozyme (Lys), the interaction between OVA and Lys in egg white at different temperatures was studied. The physical properties including turbidity, solubility and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile were analyzed. The spatial structure was characterized by circular dichroism spectroscopy, ultraviolet spectroscopy and fluorescence spectroscopy. Finally, the potential allergenicity of proteins was studied by competitive enzyme linked immunosorbent assay (ELISA). The results showed that OVA-Lys interaction during heating for 10 minutes at 60 and 65 ℃ did not significantly affect the structure and potential allergenicity of each other. However, when treated at 70 ℃, the tertiary structure of OVA was unfolded, and the hydrophobic groups of Lys were exposed outside. Thus, the interaction between OVA and Lys was formed through disulfide bonds and could significantly reduce the potential allergenicity of each other.

Key words: ovalbumin, lysozyme, interaction, structure, allergenicity

CLC Number:

TS201.2

WANG Wujing, TONG Ping, CHEN Hongbing, GAO Jinyan. Effects of Interaction on the Structure and Potential Allergenicity of Ovalbumin and Lysozyme[J]. FOOD SCIENCE, 2020, 41(6): 16-24.

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Effects of Interaction on the Structure and Potential Allergenicity of Ovalbumin and Lysozyme

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