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The impacts of four treatments ultra-high hydrostatic pressure (UHP), high pressure homogenization (HPH), combined UHP + HPH (U-H), and HPH +UHP (H-U) on bighead carp (Aristichthys nobilis) myo brillar protein (BMP) structure, functional hydrolysis property to pepsin, and antioxidant activity of hydrolysates were investigated. All treatments led to increase in low-molecular-weight BMP, the BMP stability, and hydrophobic group exposure, but decrease in total sulfhydryl content and BMP particle size, thus resulting in increased hydrolysis and antioxidant capacity of enzymatic hydrolysates. U-H treated BMP exhibited the highest surface hydrophobicity (924.5±1.0), zeta potential absolute value (18.88±0.11 mV), hydrolysis degree (54.5±1.6%), and antioxidant activity, but the lowest α-helix (21.84±2.61%), intrinsic uorescence spectrum intensity, total sulfhydryl (7.24±0.07 μmol/g), and mean particle size (182.57±2.23 nm). Therefore, U-H might be a promising pretreatment to prepare bioactive peptide.

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