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Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study
Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study
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Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study
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Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study
Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study

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Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study
Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study
Journal Article

Physicochemical properties and functional characteristics of ultrasound-assisted legume-protein isolates: a comparative study

2022
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Overview
Sonicated protein isolates were recovered from Chenopodium quinua, Phaseoulus vulgaris and Lens culinaris to develop a functional matrix by assessing the physicochemical and functional properties. The plant protein isolates were prepared from powdered materials followed by sonication in alkaline medium using a Box-Behnken design. pH (6–10), a buffer-to-material ratio (5:1 to 15:1) and sonication time (0–20 min) were taken as independent variables, whereas protein yield was taken as the dependent variable. A pH of 9, 20 min treatment, and a buffer-to-material ratio of 5:1 were the optimal extraction conditions for quinoa and black beans, whereas a 1:10 ratio was suitable for lentils. Sonication in alkaline medium caused partial protein unfolding and these isolates; in turn, the molecular weight affected the emulsifying activity and stability. Moreover, sonication had a strong effect on the gelation temperature, emulsifying activity, the water, and oil sorption. Sonication improved protein yield and exposed amino acids such as glutamic acid, aspartic acid, leucine and glycine. In turn, thiol groups were responsible for the increased in gelation temperature. The better gelling property coupled with high emulsifying property of these proteins show potential application as protein emulsifiers in the production of gels, sausages, and pet foods.