Abstract
The effect of high hydrostatic pressure (HHP) (0.1, 100, 200, 300, 400 and 500 MPa) on the structure–emulsifying relationship of scallop mantle protein was investigated. Overall, HHP could significantly change the secondary structure including the decrease of α-helix relative content and the increase of β-fold content, surface hydrophobicity, free sulfhydryl groups of scallop mantle protein. Compared with the untreated ones, scallop mantle protein had small particle size, zeta potential, solubility, and interfacial tension, as well as good emulsifying properties after proper HHP treatment. Scallop mantle protein treated at 200 MPa possessed the optimal emulsification (75.09 ± 0.50 m2/g) while it treated at 100 MPa exhibited the maximum emulsion stability (17.51 ± 0.12 min) due to high adsorbed protein content (89.25 ± 0.26%). Therefore, HHP treatment was a potential method to improve the emulsifying properties of shellfish proteins by structure modification.
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