2017
DOI: 10.1016/j.foodchem.2017.04.077
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Changes in the structure and dissociation of soybean protein isolate induced by ultrasound-assisted acid pretreatment

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Cited by 128 publications
(61 citation statements)
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“…According to the results of Table and Figure , the optimum condition was 10% (w/v) acetic acid, 70°C, and a 20 min duration. Increasing acetic acid concentration resulted in the decrease of allergenic proteins, mainly due to charge repulsion induced by acid (Huang, Ding, Dai, & Ma, ). Additionally, compared with the CSBM at relatively low temperature, the content of larger subunits was decreased when treated with high temperature (Figure ), indicating that increasing the temperature could improve the dissociation of soy proteins induced by acid.…”
Section: Resultsmentioning
confidence: 99%
“…According to the results of Table and Figure , the optimum condition was 10% (w/v) acetic acid, 70°C, and a 20 min duration. Increasing acetic acid concentration resulted in the decrease of allergenic proteins, mainly due to charge repulsion induced by acid (Huang, Ding, Dai, & Ma, ). Additionally, compared with the CSBM at relatively low temperature, the content of larger subunits was decreased when treated with high temperature (Figure ), indicating that increasing the temperature could improve the dissociation of soy proteins induced by acid.…”
Section: Resultsmentioning
confidence: 99%
“…Soy protein isolate (control, SPI) showed a typical SDS–PAGE profile of individual subunits of glycinin (A3, A4, A1,2, and BS) and β‐conglycinin (α′, α, and β) (Fig. , Lanes 2 and 6) as shown in previous studies (Arrese et al ., ; Karki et al ., ; Hu et al ., ; Huang et al ., ). The SDS‐PAGE profile of SPI was slightly altered after sonication (Fig.…”
Section: Resultsmentioning
confidence: 97%
“…Different frequency ranges can be used in HIU technology, however, to alter physical or chemical food properties a low frequency (16-100 kHz) and a large range of power (10-1000 W cm 2 ) are generally applied (Soria & Villamiel, 2010;Rastogi, 2011). Recently, power ultrasound was used to improve the functional properties of proteins (Jambrak et al, 2009;Karki et al, 2009;Chen et al, 2011;Hu et al, 2013a,b;Huang et al, 2017;. Studies have shown that HIU can break peptide bonds, destroy non-covalent interactions and change the conformation of proteins' subunits by inducing their dissociation and/or aggregation and changing therefore their functional properties (Jambrak et al, 2009;Tang et al, 2009;Martini et al, 2010;Martini & Walsh, 2012;Hu et al, 2013b).…”
Section: Introductionmentioning
confidence: 99%
“…AFM is widely used for the determination of particle size and surface morphology of proteins (Huang, Ding, Dai, & Ma, 2017).…”
Section: Discussionmentioning
confidence: 99%