Modification of ovalbumin by the enzymatic method: Consequences for foaming characteristics of fibrils

Amyloid-like fibrils from proteins possess unique functional properties for food and many other uses. This study reports the effect of different trypsin concentrations (0.1%, 0.2%, 1.0%) on the formation and foaming properties of ovalbumin protein amyloid fibrils. The fibrils were characterized through Thioflavin T (ThT) fluorescence, TEM, Circular dichroism spectroscopy, viscosity, particle size. The ThT results revealed that the moderate modification could promote protein unfolding, consequently facilitating fibril formation. Based on the results of TEM, moderate modification promoted the elongation of fibrils, and the formation of worm-like fibrils was shown. Furthermore, the structure of modified fibril aggregates was compact, which highly promoted the foaming ability and stability. According to these findings, fibrils formed by enzyme-modified OVA is a promising method that can expand the application of foaming agents and stabilizers in the food industry.

Automated summary

This study investigates the effect of different trypsin concentrations on the formation and foaming properties of ovalbumin protein amyloid fibrils. The results show that moderate modification promotes protein unfolding and elongation of fibrils, leading to the formation of worm-like fibrils. Additionally, the compact structure of modified fibril aggregates enhances foaming ability and stability. Enzyme-modified OVA fibrils could be a promising method to expand the application of foaming agents and stabilizers in the food industry.