Interfacial properties of heat-treated ovalbumin

Croguennec, Thomas; Renault, Anne; Beaufils, Sylvie; Dubois, Jean-Jacques; Pezennec, Stéphane

doi:10.1016/j.jcis.2007.07.041

Cited by 137 publications

(68 citation statements)

References 48 publications

(63 reference statements)

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“…OVA dispersions were filtered with 0.22 mm cellulose ester membrane (Millipore) in order to eliminate possible protein aggregates. OVA extinction coefficient of 0.712 L g À1 cm À1 was used in order to determinate protein concentration from the absorbance of the dispersion at 280 nm (Croguennec et al, 2007). Protein concentrations evaluated were 5, 10 and 14.2 g/L.…”

Section: Heat Treatmentmentioning

confidence: 99%

“…The instrument has a HeeNe laser as light source which operates at 632.8 nm wavelength. DLS measurements were performed at a set angle of 90 C. The refractive indexes used for solvent and OVA aggregates were 1.33 and for 1.50, respectively (Croguennec et al, 2007). The mean hydrodynamic diameter (nm) was obtained from the peak of the intensity particle size distribution (PSD) (Carvalho, Carvalho, Alves, & Tabak, 2013).…”

Section: Particle Size Distributionmentioning

confidence: 99%

“…OVA is a globular protein of 43 kDa molecular weight and it is composed by 385 aminoacids, of which a half is hydrophobic and mainly buried into the protein structure. Otherwise, charged aminoacids (a third part of total aminoacids) are mainly located on protein surface in contact with aqueous medium (Croguennec, Renault, Beaufils, Dubois, & Pezennec, 2007;Giosafatto et al, 2012). OVA has one disulphide bond and four free sulfhydryl groups.…”

Section: Introductionmentioning

confidence: 99%

“…The effect of heat treatment on the OVA molecular structure has been extensively studied (Galazka et al, 1999;Hayakawa & Nakai, 1985;Matsudomi, Takahashi, & Miyata, 2001;Nakamura, Sugiyam, & Sato, 1978;Nyemb et al, 2014;Weijers et al, 2003). Heating promotes protein unfolding, phenomenon known as denaturation, in which hydrophobic aminoacids are exposed conferring an increase in protein surface hydrophobicity (Croguennec et al, 2007;Weijers et al, 2003). Environment conditions under which denaturation take place can lead to OVA aggregation.…”

Section: Introductionmentioning

confidence: 99%

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Section: Heat Treatmentmentioning

confidence: 99%

Section: Particle Size Distributionmentioning

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Section: Introductionmentioning

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“…The 59 foaming properties of WPI are influenced by protein concentration, pH, high pressure, 60 thermal treatment, foam procedure, by their nature and behaviour at interfaces (denaturation, 61 protein-protein interactions) and by their interactions with other food ingredients (Bouaouina 62 et al, 2006;Croguennec et al, 2007;Damodaran, 1996Damodaran, , 2005Ibanoglu and Karatas¸ 2001; 63 Linden and Lorient, 1999; Pittia et al, 1996;Schmitt et al, 2007; Vaclavik and Christian, 64 2008; Zhu and Damodaran, 1994). 65…”

Section: Introduction 51mentioning

confidence: 99%

Fibrillization of whey proteins improves foaming capacity and foam stability at low protein concentrations

Oboroceanu

Wang

Magner

et al. 2014

Journal of Food Engineering

105

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26The foaming properties of fibrillar whey proteins were compared with those of native or 27 denatured whey proteins and also with egg white protein. Whey protein foaming capacity and 28 stability were related to protein concentration, pH, time of whipping, pressure and heating 29 treatments. Foams produced from fibrils showed significant improvement in foaming capacity 30 and stability when compared with non-fibrillar whey proteins. Dynamic high shear 31 (microfluidization) or moderate shear (Ultra-turrax mixing) of fibrillar protein dispersions did 32 not significantly affect their subsequent foaming properties. Furthermore, foams prepared 33 with fibrillar whey protein (≤ 3% protein) had comparable capacity and stability to that from 34 egg white protein, which is the traditional foaming ingredient in food industry. Results 35 suggest that fibrillized whey proteins are highly effective foaming agents even at relatively 36 low protein concentrations (1-3% w/w). Introduction 51Whey protein isolate (WPI) and egg white protein (EWP) are often used as foaming agents in 52 the food industry in the manufacture of meringues, cake, whipped toppings and leavened 53 bakery products (Campbell and Mougeot, 1999;Damodaran, 1996Damodaran, , 1997 Davis and 54 Foegeding, 2007; Kuropatwa et al., 2009; Linden and Lorient, 1999; Nicorescu et al., 2009a Nicorescu et al., , 55 2009b Vaclavik and Christian, 2008; van der Plancken et al., 2007). 56Previous studies have shown that WPI or EWP can improve and maintain the quality (texture, 57 volume) of "foamed" food, in particular foaming capacity and stability (Davis and Foegeding, 58 2004; Doi and Kitabake, 1997; Kuropatwa et al., 2009; Vaclavik and Christian, 2008). The 59 foaming properties of WPI are influenced by protein concentration, pH, high pressure, 60 thermal treatment, foam procedure, by their nature and behaviour at interfaces (denaturation, 61 protein-protein interactions) and by their interactions with other food ingredients (Bouaouina 62 et al., 2006;Croguennec et al., 2007;Damodaran, 1996Damodaran, , 2005Ibanoglu and Karatas¸ 2001; 63 Linden and Lorient, 1999; Pittia et al., 1996;Schmitt et al., 2007; Vaclavik and Christian, 64 2008; Zhu and Damodaran, 1994). 65The stability of foams is affected by numerous factors such as the protein adsorption from 66 solution at the liquid/gas interface, the surface rheological properties, diffusion of the gas out 67 and into foam cells, size distributions of the cells, liquid surface tension, external pressure and 68 temperature (Morrison and Ross, 2002). Foams are destabilized by drainage that causes 69 thinning of the interstitial liquid film and by its rupture (Stainsby, 1986; Hamley, 2000). The 70 drainage of the liquid will depend on the physical properties of the liquid, particularly 71 viscosity. As the liquid drains from the foam, the bubbles will coalesce. The coalescence can 72 be stabilized by the presence of the proteins at the liquid/air interface that can modify the 73 surface tensio...

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Functional Properties of Egg Components in Food Systems

Mine

Yang

2010

Handbook of Poultry Science and Technology

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Interfacial properties of heat-treated ovalbumin

Cited by 137 publications

References 48 publications

Impact of environment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs

Impact of environment conditions on physicochemical characteristics of ovalbumin heat-induced nanoparticles and on their ability to bind PUFAs

Fibrillization of whey proteins improves foaming capacity and foam stability at low protein concentrations

Functional Properties of Egg Components in Food Systems

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