Abstract

The plum seed protein isolates (PSPI), wolfberry protein isolates (WPI) jujube seed protein isolates (JPI), and hemp seed protein isolates (HPI) were prepared and treated with high-pressure homogenization at 90 MPa. The effects of high-pressure homogenization treatment on particle size, surface hydrophobicity, solubility, subunits, rheological behavior, and microstructure of proteins were investigated in this study. As compared with native proteins, the particle size of PSPI, WPI, JPI and HPI decreased 89%, 38%, 93% and 83%, respectively, after high-pressure homogenization treatment; the solubility of PSPI, WPI, JPI and HPI increased 31%, 9%, 43% and 201%, respectively. However, the effects of treatment on surface hydrophobicity and rheological behavior depended on the type of proteins. The surface hydrophobicity of WPI increased 22%, while the surface hydrophobicity of PSPI, JPI and HPI decreased 4%, 19% and 46%, respectively. The treatment also promoted the gelation of WPI, JPI and HPI. Furthermore, the composition of proteins was not affected by high-pressure homogenization treatment.

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