Fabrication mechanism and functional properties of ovalbumin fibrils prepared by acidic heat treatment

Abstract

AbstractBACKGROUNDOvalbumin (OVA), accounting for 50% of proteins in egg white, is a kind of high‐quality protein with excellent nutritional and processing functions. Acid heat treatment will induce the deformation and filtration of OVA, endowing it with improved functionality. However, the molecular kinetic process during the fibrillation of OVA and the application of the fabricated OVA fibrils (OVAFs) have not been thoroughly studied and revealed.RESULTSIn this study, the fabrication mechanism and the application OVAFs as an interfacial stabilizer and polyphenol protector were investigated. Acidic (pH 3.0) heat treatment was used to induce the fibrillation of OVA, and thioflavin T fluorescence intensity, molecular weight distribution, and the tertiary and secondary structures of OVAF samples were recorded to determine the fibrillation efficiency and the molecular mechanism. The results showed that, in the initial stage of fibrillation, OVA first hydrolyzed to oligopeptides, accompanied by the exposure of hydrophobic domains. Then, oligopeptides were connected by disulfide bonds to form primary fibril monomers. Hydrophobic interaction and hydrogen bonding may participate in the further polymerization of the fibrils. The fabricated OVAFs were characterized by a β‐sheet‐rich structure and possessed improved emulsifying, foaming, and polyphenol protection ability.CONCLUSIONThe research work was meaningful for exploring the application of globular water‐soluble OVA in an emerging nutritious food with novel texture and sensory properties. © 2023 Society of Chemical Industry.