2015
DOI: 10.1016/j.foodhyd.2014.10.010
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Changes in functionality of whey protein and micellar casein after high pressure – low temperature treatments

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Cited by 24 publications
(11 citation statements)
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“…The presence of WPs could inhibit the formation of CN flocs through a delay in the development of hydrophobic and hydrogen interactions in flocs. Consequently, CN solubility increased in the presence of WPs under pressurization at subzero temperatures (Baier, Purschke, et al, 2015;Baier et al, 2015aBaier et al, , 2015b.…”
Section: Effect Of Medium Composition (Wps and Lactose)mentioning
confidence: 99%
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“…The presence of WPs could inhibit the formation of CN flocs through a delay in the development of hydrophobic and hydrogen interactions in flocs. Consequently, CN solubility increased in the presence of WPs under pressurization at subzero temperatures (Baier, Purschke, et al, 2015;Baier et al, 2015aBaier et al, , 2015b.…”
Section: Effect Of Medium Composition (Wps and Lactose)mentioning
confidence: 99%
“…This results from the interaction between β-LG and κ-CN. Unfolded β-LG can form disulfide-bonded aggregates with κ-CN via thioldisulfide bond exchange (Baier et al, 2015a;Bravo et al, 2013Bravo et al, , 2012. These exchanges resulted in greater denaturation of β-LG and α-LA in milk than in whey or buffer, potentially due to the smaller number of molecules available for interaction or aggregation, owing mainly to the absence of CN in whey (Huppertz et al, 2019;Mazri, Ramos, et al, 2012;Patel & Huppertz, 2014).…”
Section: 21mentioning
confidence: 99%
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“…Application of high pressure treatments can induce milk protein denaturation, causing structural modifications of both CN and WPs [3,10,54,63,116,134]. The impact of high pressure treatment on WPs has recently been reviewed by Piccolomini, Kubow and Lands [108].…”
Section: Influence Of Food Processing On the Release Of Bioactive Pepmentioning
confidence: 99%