LAUSR

Abstract The effects of ultrasound with different powers (0-500 W) on the structure and stability of protein from sea cucumber gonad were investigated, according to the changes in phenylalanine (Phe), α-helix, β-sheet, tryptophan (Trp), surface hydrophobicity, particle size distribution, microstructure and amino acid (AA). With the increase in ultrasound power, the contents of Phe, β-sheet and Trp, surface hydrophobicity and particle size first increased and then decreased, while α-helix content was opposite. Compared with the non-ultrasound group, the content of α-helix and random coil significantly decreased by 24.71% and 22.33% in the 200 W ultrasound group, while Phe content, β-sheet content, fluorescence intensity (FI), the surface hydrophobicity and hydrophobic AA significantly increased by 12.77%, 75.91%, 7.90%, 15.61% and 7.00%, respectively (P