2008
DOI: 10.1016/j.foodhyd.2007.05.017
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Effect of dynamic high pressure on whey protein aggregation: A comparison with the effect of continuous short-time thermal treatments

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Cited by 95 publications
(59 citation statements)
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References 70 publications
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“…However, a posterior study carried out by the same research group showed that UHPH induces irreversible disruption of Food Eng Rev large whey protein aggregates without affecting their conformation and their concomitant solubility; in addition, UHPH-treated whey proteins showed better foaming and stabilising properties [3]. Whey protein aggregation results from a combined effect of mechanical forces and short-life heating phenomena, but protein aggregates remain ''soluble'' [28]. Various studies have proven that processing of casein micelles by UHPH can modify casein micelle organisation with an enhancement of their binding capacity to triclosan, a-tocopherol acetate or curcumin [2,9,58].…”
Section: Particle Disruption and Food Stabilitymentioning
confidence: 99%
See 1 more Smart Citation
“…However, a posterior study carried out by the same research group showed that UHPH induces irreversible disruption of Food Eng Rev large whey protein aggregates without affecting their conformation and their concomitant solubility; in addition, UHPH-treated whey proteins showed better foaming and stabilising properties [3]. Whey protein aggregation results from a combined effect of mechanical forces and short-life heating phenomena, but protein aggregates remain ''soluble'' [28]. Various studies have proven that processing of casein micelles by UHPH can modify casein micelle organisation with an enhancement of their binding capacity to triclosan, a-tocopherol acetate or curcumin [2,9,58].…”
Section: Particle Disruption and Food Stabilitymentioning
confidence: 99%
“…Particle size profiles of food emulsions have proven that UHPH applied to protein suspensions can lead to protein aggregates of \100 nm and oil-in-water emulsions of submicron droplet diameters, which is in the size domain of nano-particles [8,10,25,28,32]. However, during UHPH above 200 MPa, part of the energy is dissipated as heat, which may collapse oil droplets, resulting in rheological properties comparable to untreated emulsions of corn oil stabilised by commercial micellar casein [63].…”
Section: Particle Disruption and Food Stabilitymentioning
confidence: 99%
“…As the intensity of the heat treatment increases, the whey proteins unfold, aggregate and form sediments through a multiple-reaction process. In general, for protein precipitation, the authors recommend to adjust the pH of whey between 6.3 and 6.8 using NaOH solution, then heat it to 90 °C and acidize it to pH between 4.5 and 5.5 [9,10].…”
Section: Optimization Of Proteins Recovery Process From Cheese Whey 142mentioning
confidence: 99%
“…Denaturation/aggregation phenomena depend on physical and biochemical parameters, such as heating temperature and holding time, heating rate, presence of proteins or other hydrocolloids, protein concentration, pH, ionic strength and mineral content [5,7,9]. Even though there are many studies about the optimization of the process of aggregation of whey proteins, no results were found about the influence of the presence of residual fat on it.…”
Section: Optimization Of Proteins Recovery Process From Cheese Whey 142mentioning
confidence: 99%
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