2012
DOI: 10.1016/j.foodhyd.2011.11.006
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Stability and mechanism of whey protein soluble aggregates thermally treated with salts

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Cited by 139 publications
(100 citation statements)
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“…This result agrees with previous works, whereas the higher fat content in samples appeared to inhibit the flocculant action [17].…”
Section: Yield and Water Retention Of Protein Aggregatessupporting
confidence: 93%
“…This result agrees with previous works, whereas the higher fat content in samples appeared to inhibit the flocculant action [17].…”
Section: Yield and Water Retention Of Protein Aggregatessupporting
confidence: 93%
“…33 This phenomenon is common in protein solutions because protein solubility can be strongly affected by the pH and ionic strength of the medium. 34 The zein NPs prepared in this study exhibited a slow T4OL release rate, which is of interest because the skin behaves as a natural barrier that protects the body against the external environment and the permeation of substances. 3 Therefore, in the case of slow release, the active compound will have sufficient time to penetrate into the skin and into the cells.…”
Section: Resultsmentioning
confidence: 93%
“…For studies of protein unfolding, denaturation and production of soluble protein aggregates, WPI solution at 3% (w/w) was prepared with final pH adjusted to 6.8 with 1 M of NaOH (Merck, Germany). It has been shown that, when WPI solutions of low protein concentration (1e3%) heated under neutral pH, small amounts of added salts, lead to the formation of soluble protein aggregates via both disulfide and hydrophobic interactions (Purwanti et al, 2011;Ryan et al, 2012;Schmitt, Bovay, Rouvet, Shojaei-Rami, & Kolodziejczyk, 2007). For the development of protein gel, was used the WPI solution at 10% (w/w) and final pH was adjusted to 3.0 with 1 M of HCl (Merck, Germany).…”
Section: Whey Protein Solutionsmentioning
confidence: 99%