The oyster protein was ball milling treated in this work, and the effects on particle size, conformation, physicochemical properties, and in vitro protein digestibility (IVPD) were investigated. After ball milling treatment, the particle size obviously decreased, and the protein powder became denser and more homogeneous. The ball milling treatment could not change the primary structure of oyster protein. However, it could affect the secondary structure and physicochemical properties. The disulfide bond increased from 8.18 to 9.14 μmol/g protein, while the protein surface hydrophobicity index increased from 0.088 to 0.176. The decreasing water‐holding capacity from 390% to 226% and the increasing oil‐binding capacity from 91.2% to 189.1% were related to the alterations of conformation and physicochemical properties. Ball milling could also improve the IVPD from 54.6% to 82.4%. These results provided theoretical basis for the application of ball milling treatment in the utilization of oyster protein in the food industry.

In this study, the effects of limited hydrolysis and/or high-pressure homogenization (HPH) treatment in acid conditions on the functional properties of oyster protein isolates (OPI) were studied. Protein solubility, surface hydrophobicity, particle size distribution, zeta potential, foaming, and emulsifying properties were evaluated. The results showed that acid treatment led to the dissociation and unfolding of OPI. Subsequent treatment such as limited proteolysis, HPH, and their combination remarkably improved the functional properties of OPI. Acid treatment produced flexible aggregates, as well as reduced particle size and solubility. On the contrary, limited hydrolysis increased the solubility of OPI. Furthermore, HPH enhanced the effectiveness of the above treatments. The emulsifying and foaming properties of acid- or hydrolysis-treated OPI significantly improved. In conclusion, a combination of acid treatment, limited proteolysis, and HPH improved the functional properties of OPI. The improvements in the functional properties of OPI could potentiate the use of oyster protein and its hydrolysates in the food industry.