Effects of Ultrasonic Treatment on the Structure, Functional Properties of Chickpea Protein Isolate and Its Digestibility In Vitro
Shihua Kang, Jian Zhang, Xiaobing Guo, Yongdong Lei, Mei Yang
Foods
Abstract
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.
Extracted Claims
5 claims extracted from this paper into the knowledge graph
ultrasonic treatment causes disulfide bond of CPI to be opened
“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.”
ultrasonic treatment improves emulsification and foaming stability of CPI
“The emulsification and foaming stability of CPI were significantly improved after ultrasonic treatment.”
ultrasonic treatment exposes hydrophobic amino acid residues
“The changes in surface hydrophobicity of CPI indicated that ultrasound treatment exposed more hydrophobic amino acid residues.”