2011
DOI: 10.1016/j.foodhyd.2011.02.027
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Modulation of rheological properties by heat-induced aggregation of whey protein solution

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Cited by 70 publications
(43 citation statements)
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“…It was found that neither an endothermic nor an exothermic curve but a line similarly horizontal between 50 and 90 o C, which meant the PWP was mostly polymerized and barely affected by heat from 50 ~ 90ºC, and such a conc lusion was in accordance with the previous research [Purwanti et al, 2011]. Therefore, the PWP may have thermal stabilities in this temperature range, and the DSC curve provides the sterilization temperature range (lower than 90 o C) for low-fat yogurt containing PWP as a fat replacer.…”
Section: Thermal Analysis Of Polymerized Whey Proteinsupporting
confidence: 89%
See 1 more Smart Citation
“…It was found that neither an endothermic nor an exothermic curve but a line similarly horizontal between 50 and 90 o C, which meant the PWP was mostly polymerized and barely affected by heat from 50 ~ 90ºC, and such a conc lusion was in accordance with the previous research [Purwanti et al, 2011]. Therefore, the PWP may have thermal stabilities in this temperature range, and the DSC curve provides the sterilization temperature range (lower than 90 o C) for low-fat yogurt containing PWP as a fat replacer.…”
Section: Thermal Analysis Of Polymerized Whey Proteinsupporting
confidence: 89%
“…Heat treatment makes soluble whey protein aggregates formed at concentrations (10%, w/w, in our study) below their critical gelation concentration, which is approximately 12% [Purwanti et al, 2011]. The solu ble aggregates should be small and roughly spherical, have high surface charge, and low surface hydrophobicity for maximum thermal stability [Wijayanti et al, 2014].…”
Section: Thermal Analysis Of Polymerized Whey Proteinmentioning
confidence: 77%
“…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%
“…These include the protein type (molecular mass and amino acid composition) (6), protein hydrophobicity and free sulphydryl groups (7), protein concentration (8), the proportions of individual whey proteins in the mixture (9), the type and amount of salts (8,10,11), lipids (12), lactose (6), sucrose (13) present in the formula-tion, process conditions (pH, temperature, heating and cooling rate) (14,15), and/or specific treatments such as microparticulation of whey proteins (16)(17)(18). Among these factors, attention has been focused on protein concentration and pH.…”
Section: Introductionmentioning
confidence: 99%