Changes in structural and functional properties of whey protein cross-linked by polyphenol oxidase

[Display omitted] •Cross-linked Whey protein by polyphenol oxidase to form dimers and polymers.•Cross-linked whey protein changed the structure and spatial conformation of protein.•Cross-linked whey protein enhanced the foaming and oxidation resistance of protein.•Cross-linked whey protein inhibited the emulsification of protein. The natural whey protein is unstable, to achieve more efficient utilization, the functional properties of whey protein were modified by changing its structure, and enzymatic cross-linking is one of the common methods in dairy products to change the functional characterization. This study was conducted with objective to evaluate the structural and functional of whey protein which was cross-linked by polyphenol oxidase from Agaricus bisporus. Whey protein was cross-linked by polyphenol oxidase, and the polymers and dimers were revealed by SDS-PAGE and LC-MS/MS, the structural alterations of the polymers were analyzed by UV–vis, fluorescence spectroscopy and SEM, and the effects of functional properties of whey protein after cross-linked were also explored. Results showed that dimer and high polymer of β-lactoglobulin were formed, the secondary structure of whey protein was exhibited a significant variation, and the microstructure changed obviously. Moreover, the foaming and antioxidant activity of whey protein was enhanced although the emulsifying was reduced after cross-linked. These findings emphasize the feasible application of enzymatic cross-linking in improving the functional properties of whey protein, and provide a new direction for changing the traditional processing technology of whey protein and developing high-quality products.