Effects of Ultrasonic Treatment on the Structure, Functional Properties of Chickpea Protein Isolate and Its Digestibility In Vitro

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.

Influence of pre‐treatment methods on quality indicators and mineral composition of plant milk from different sources of raw materials

“…These changes affect the dispersion of protein molecules or, rather, lead to a decrease in distribution, facilitating the mass transfer of the protein phase into the solution. The mechanical impact of ultrasonic cavitation at the molecular level is accompanied by partial denaturation of proteins and conformational changes in secondary and tertiary structures 40,41 . The proteins are unraveled and hydrophobic cores rich in phenylalanine, tyrosine and tryptophan are exposed, which increases the hydrophobicity of the surface 42 .…”

“…The mechanical impact of ultrasonic cavitation at the molecular level is accompanied by partial denaturation of proteins and conformational changes in secondary and tertiary structures. 40,41 The proteins are unraveled and hydrophobic cores rich in phenylalanine, tyrosine and tryptophan are exposed, which increases the hydrophobicity of the surface. 42 With an increase in the time of sonication, a decrease in the yield of dry substances is observed by an average of 10%, as well as carbohydrates by an average of 20% (Table 3).…”

Effect of ultrasonic frequency on the structural and functional properties of pea protein isolation

“…33 Hence, the adsorption capacity of the overmodified protein at the air-water interface was reduced, thus worsening its foaming properties. 34…”

Advances on the Antioxidant Peptides from Nuts: A Narrow Review

“…Protein quality is defined based on the amino acid pattern and percent of digestibility of proteins. In vitro protein digestibility was carried out by a version of the method of Kang et al [ 17 ]. The digestibility for nut proteins has been estimated to be approximately above 70% in Table 1 , which is higher than that of other plant proteins, such as wheat digestibility which is 46%.…”