2011
DOI: 10.1007/s11947-011-0674-8
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Hydroxyl Radical-Stressed Whey Protein Isolate: Functional and Rheological Properties

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Cited by 33 publications
(30 citation statements)
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“…This could be due to the broader range of molecular weights available: one could therefore, expect that the packing density at the interface would be higher, with the low molecular weight species filling in the gaps in the interfacial layer. Such a non-monotonic evolution of the interfacial properties of proteins with gradually increasing the level of oxidation had already been reported elsewhere: Kong et al [38] found that moderate oxidation improved the foaming and emulsifying properties of whey proteins, although only up to a certain oxidation level, after which the performance of whey proteins in that respect decreased. A similar effect was also recently observed with soy proteins [21], and it was hypothesized to be caused by increased surface hydrophobicity due to partial protein unfolding, as well as by a reinforcing effect of a limited amount of small protein aggregates within the interfacial film.…”
Section: Interfacial Activity Of Oxidized Whey Proteinssupporting
confidence: 73%
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“…This could be due to the broader range of molecular weights available: one could therefore, expect that the packing density at the interface would be higher, with the low molecular weight species filling in the gaps in the interfacial layer. Such a non-monotonic evolution of the interfacial properties of proteins with gradually increasing the level of oxidation had already been reported elsewhere: Kong et al [38] found that moderate oxidation improved the foaming and emulsifying properties of whey proteins, although only up to a certain oxidation level, after which the performance of whey proteins in that respect decreased. A similar effect was also recently observed with soy proteins [21], and it was hypothesized to be caused by increased surface hydrophobicity due to partial protein unfolding, as well as by a reinforcing effect of a limited amount of small protein aggregates within the interfacial film.…”
Section: Interfacial Activity Of Oxidized Whey Proteinssupporting
confidence: 73%
“…The rate of carbonyl formation then progressively declined, reaching a plateau of around 50 mmol/kg soluble protein after 48 h incubation. The last measurement point at 168 h incubation showed a value slightly below this plateau, which may be due to extensive modification, aggregation, and loss of solubility of the proteins [5,38].…”
Section: Experimental Designmentioning
confidence: 92%
“…Kong et al . () showed that a sharp decline in the solubility of WPI attacked by •OH could have resulted from structural changes. The samples with cryoprotectants and protein hydrolysates had less solubility loss than the control samples, indicating that cryoprotectants and WPI hydrolysates can reduce the myofibril complex structural changes that were induced by protein oxidation.…”
Section: Resultsmentioning
confidence: 99%
“…The oxidation of proteins also involves a specific sector of the research that aims to selectively modify proteins and their functionality (Liu, Xiong, & Butterfield, 2000;Chen, Zhao, Sun, Ren, & Cui, 2013;Cui, Xiong, Kong, Zhao, & Liu, 2012;Kong, Xiong, Cui, and Zhao, 2013). Among oxidising agents capable of modify macromolecules, ozone, that is also included in the most reactive plasma species, has been recently applied for cassava starch (Klein et al, 2014), wheat starch (Sandhu, Manthey, & Simsek, 2012), cocoyam and yam starches (Oladebeye, Oshodi, Amoo, & Karim, 2013), egg and whey proteins (Uzun, Ibanoglu, Catal, & Ibanoglu, 2012;Segat et al, 2014).…”
Section: Accepted Manuscriptmentioning
confidence: 99%