High-pressure homogenization influences the functional properties of protein from oyster (Crassostrea gigas)

In this study, the effects of high-pressure homogenization (HPH) (20, 60, and 100 MPa) on the structure, microstructure, and functional properties of oyster (Crassostrea gigas) protein (CGP) were investigated. Circular dichroism examination showed that the secondary structure of oyster proteins became loose and that the α-helix transformed into a random coil structure. The fluorescence spectra had a redshift from 350 nm to 360 nm, exposing the chromophore and changing the tertiary structure of CGP. With the increase in homogeneous pressure, HPH significantly reduced particle sizes of CGP. Compared to other treatments, HPH at 100 MPa showed a higher surface hydrophobic index (86.84), solubility (84.7%), and water holding capacity (15.2 g/g). However, the emulsion activity index (137.5 m2/g) and foaming ability (113.3%) were best at a lower pressure (20 MPa). The scanning electron microscope showed that HPH treatment could improve emulsion stability. This work demonstrates that HPH treatment has a positive impact on the physicochemical and functional properties of CGP for potential industrial applications.