2020
DOI: 10.1016/j.jcs.2020.103076
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Modifications of physicochemical and functional properties of amaranth protein isolate (Amaranthus cruentus BRS Alegria) treated with high-intensity ultrasound

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Cited by 39 publications
(37 citation statements)
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“…2 ) made the protein molecules denatured or reaggregated to new aggregation, so the turbidity increased. Similar phenomena were also observed in other study [43] .…”
Section: Resultssupporting
confidence: 92%
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“…2 ) made the protein molecules denatured or reaggregated to new aggregation, so the turbidity increased. Similar phenomena were also observed in other study [43] .…”
Section: Resultssupporting
confidence: 92%
“…It was reported that high solubility could promote the diffusion of oil–water interface and EAI increased [40] . The unfolding of globular amaranth isolated proteins was promoted by high-intensity ultrasonic treatment, and the nonpolar groups were exposed with the increment of surface activity [43] . The study found that ultrasonic treatment improved emulsification properties by reducing particle size of pea proteins [61] .…”
Section: Resultsmentioning
confidence: 99%
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“…Ultrasound treatment can cause the protein structure to refold and reaggregate (L. Huang, Zhang, Yan, Ma, & Ma, 2020). Ultrasound reduced the particles size in aqueous dispersions of protein, indicating the dissociation of aggregates from protein (Constantino & Garcia‐Rojas, 2020; Y. Li et al, 2020). The frequency and working mode of ultrasound can change the structure of protein significantly, including the secondary and tertiary structure and particles.…”
Section: Ultrasonic‐aided Modification Of Food Proteinmentioning
confidence: 99%
“…reduced the particles size in aqueous dispersions of protein, indicating the dissociation of aggregates from protein(Constantino & Garcia- Rojas, 2020;. The frequency and working mode of ultrasound can change the structure of protein significantly, including the secondary and tertiary structure and particles.…”
mentioning
confidence: 99%