Physicochemical properties of hydrophobic and hydrophilic peptides from oyster protein

Summary The physicochemical properties of the hydrophilic peptides (HIPs) and the hydrophobic peptides (HOPs) from the oyster protein hydrolysates (OPHs) were analysed. The technology of high‐performance liquid chromatography and dynamic light scattering was used to determine the molecular weights and the particle sizes of HIP and HOP. About 60–70% of them had a molecular weight below 500 Da and the particle size was all about 100 nm, which were smaller than OPH. Furthermore, compared with OPH and HIP, HOPs have obvious advantages in surface hydrophobic and emulsifying properties because they have more hydrophobic groups on the surface. The emulsifying activity and emulsion stability of HOP can be significantly improved from 3.80 to 42.88 m 2 g −1 and 131.17–163.70 min, respectively, because of its high surface hydrophobicity. Thus, our results suggest that HOPs have a great potential to be developed as an emulsifier.