This study evaluated the effects of different levels of ultrasonic power (200, 400, 600 W) and treatment time (0, 10, 15 and 30 min) on the structure, emulsification characteristics, and in vitro digestibility of chickpea protein isolate (CPI). The changes in surface hydrophobicity of CPI indicated that ultrasound treatment exposed more hydrophobic amino acid residues. The analysis of sulfhydryl content and zeta potential showed that ultrasound caused the disulfide bond of CPI to be opened, releasing more negatively charged groups, and the solution was more stable. In addition, Fourier Transform Infrared Spectroscopy (FT-IR) and intrinsic fluorescence spectroscopy showed that ultrasound changes the secondary and tertiary structure of CPI, which is due to molecular expansion and stretching, exposing internal hydrophobic groups. The emulsification and foaming stability of CPI were significantly improved after ultrasonic treatment. Ultrasonic treatment had a minor effect on the solubility, foaming capacity and in vitro digestibility of CPI. All the results revealed that the ultrasound was a promising way to improve the functional properties of CPI.

This study aimed to investigate the effect of phosphorylation on the structure and emulsification of Coregonus peled, Esox lucius and Grass carp scale gelatin. Fourier transform infrared spectroscopy (FTIR) and endogenous fluorescence spectra showed that the structures of the three fish scale gelatins changed. Additionally, the surface hydrophobicity index of the three fish scale gelatins increased by 36.72, 31.42 and 111.67, respectively, after 1 h of phosphorylation, and the surface tension decreased by 17.27, 32.58 and 18.7 mN/m, respectively. The emulsification activity index increased by 115.86, 155.22 and 45.52 m²/g, and the emulsification stability index increased by 98.37, 256.77 and 169.61 min, respectively. The structure of fish scale gelatin changed after phosphorylation, which resulted in the improvement of emulsification. This work will provide useful information to understand the relationship between the structure and function of gelatin.