Optimizing yeast protein properties through moderate high-pressure homogenization: A study on structural and...

Yeast protein is a sustainable alternative to conventional proteins, but its application requires functional optimization. This study evaluated the effects of high-pressure homogenization on the structural, functional, and flavor-binding properties of yeast protein. Moderate high-pressure homogenization (60-90 MPa) yielded optimal results, however, excessive pressure (120 MPa) caused re-aggregation. Specifically, compared with the untreated sample, the protein treated under 60 MPa exhibited a decrease in the radius of gyration from 29.11 ± 0.86 nm to 24.47 ± 1.00 nm and a reduction in turbidity by 30.56%. Moderate treatment significantly enhanced water-binding capacity, gel elasticity, antioxidant activity, and digestibility. Furthermore, high-pressure homogenization improved flavor-binding ability by exposing internal aromatic residues. Molecular docking revealed that hydrogen bonding and hydrophobic interactions play critical roles in flavor compound binding. These findings suggest that moderate high-pressure homogenization is a promising strategy to improve the functional properties of yeast protein for various food applications.