Gelation of oil-in-water emulsions stabilized by whey protein

Mantovani, Raphaela Araújo; Cavallieri, Ângelo Luiz Fazani; Cunha, Rosiane L.

doi:10.1016/j.jfoodeng.2015.12.011

Cited by 46 publications

(20 citation statements)

References 37 publications

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“…In the present work, no heat treatment was used; still, a strong self-supporting gel was formed by acidification of WPI NEs to pH 5. The improvement in firmness of the gel could be attributed to the nanoscale droplet size of our NEs compared to microscale droplets of both Rosa et al 22 and Mantovani et al’s 25 emulsions. Ye and Taylor 26 also showed that the storage modulus of a WPI emulsion gel, made by acidification of a preheated WPI emulsion, increased with a decrease in the average droplet size.…”

Section: Results and Discussionmentioning

confidence: 71%

“…The authors proposed that heating the whey protein solution was essential to form a self-supporting gel. Recently, 1 Mantovani et al 25 reported that acidification of a 5% WPI-stabilized 30% oil-in-water emulsion did not form a gel, whereas mixing with a heat-treated 5% WPI before acidification led to a self-supporting gel. In contrast, Ye and Taylor 26 were able to form whey protein-stabilized emulsion gel by heating an emulsion followed by acidification, without the need for adding additional heat-treated protein to form an emulsion-filled gel.…”

Section: Results and Discussionmentioning

confidence: 99%

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Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions

et al. 2019

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This research aimed to investigate the possibility of forming gelled nanoemulsions (NEs) by inducing attractive interactions among the nanodroplets. The effect of salt concentration and changes in pH on the stability and gelation behavior of 2, 4, and 5% sodium caseinate (SC) and whey protein isolate (WPI)-stabilized 40% canola oil-in-water NEs were investigated. For the effect of salt, sodium chloride was added in a concentration of 0.1, 0.5, and 1 M in the continuous phase of the NEs at neutral pH, whereas to study the effect of acidification, the pH of the NEs was adjusted to the isoelectric point (pI) of the proteins. The addition of salt led to attractive gelation in WPI NEs because of a screening of charge. In contrast, the gel strength of SC-stabilized NEs was reduced with salt, which was attributed to the loss of close packing of droplets and their surrounding repulsive barriers because of charge screening and to the steric barrier of interfacial SC preventing droplet aggregation. All the NEs with pH at the pI of proteins transformed into strong attractive gels made of droplet aggregates irrespective of the type or concentration of protein because of the complete charge neutralization. The strength of the acidified NE gels increased with a decrease in droplet size and the type of protein used. Overall, research on the effect of different environmental factors on the stability and gelation behavior of protein-stabilized NEs could be useful for possible applications of these nanoscale materials in various food systems.

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Section: Results and Discussionmentioning

confidence: 71%

Section: Results and Discussionmentioning

confidence: 99%

Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions

et al. 2019

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“…2), resulting in stronger network. One reason might be that smaller droplets could easily enter into the gel matrix of soy protein emulsion that improved the network structure (Mantovani et al ., 2016). Another reason could be due to that the decrease of droplets size resulted in the increase of total surface area but the decrease of the space between droplets, leading to the enhancement of interactions between surface protein and gel network protein (Mcclements et al ., 1993).…”

Section: Resultsmentioning

confidence: 99%

Effects of different nut oils on the structures and properties of gel‐like emulsions induced by ultrasound using soy protein as an emulsifier

Geng

Zhou

et al. 2020

Int J of Food Sci Tech

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“…It is well known that whey proteins form cross-links under heating. When heat is gently applied, the emulsions form soft solids [11] with a very special mouthfeel.…”

Section: Introductionmentioning

confidence: 99%

Milk Emulsions: Structure and Stability

Braun

Hanewald

Vilgis

2019

Foods

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The main aim of this research is to investigate the characteristics of milk and milk proteins as natural emulsifiers. It is still largely unclear how the two main fractions of the milk proteins behave as emulsifier in highly concentrated emulsions. The surface-active effect of these is determined experimentally for emulsions with a high oil content (φ > 0.7), in this case fully refined rapeseed oil. Recent publications have not yet sufficiently investigated how proteins from native milk behave in emulsions in which a jamming transition is observed. In addition, scientific measurements comparing fresh milk emulsions and emulsions of dried milk protein powders based on rheological and thermal properties are pending and unexamined. The emulsions, prepared with a rotor-stator disperser, are investigated by their particle size and analysed by microscopy, characterised by their rheological properties. The behaviour under shear is directly observed by rheo-optical methods, which enables the direct observation of the dynamic behaviour of the oil droplets undergoing a size selective jamming transition. For a better understanding of the contributions of the different emulsifying proteins, oil-in-water emulsions have been prepared by using whey protein isolates and sodium casinates. Their different role (and function) on the interface activity can be assigned to the droplet sizes and mechanical behaviour during increasing shear deformation. In addition, solid (gelled) emulsions are prepared by heating. It is shown that the cysteine-containing whey proteins are mainly responsible for the sol–gel transition in the continuous water phase and the formation of soft solids.

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Gelation of oil-in-water emulsions stabilized by whey protein

Cited by 46 publications

References 37 publications

Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions

Salt and pH-Induced Attractive Interactions on the Rheology of Food Protein-Stabilized Nanoemulsions

Effects of different nut oils on the structures and properties of gel‐like emulsions induced by ultrasound using soy protein as an emulsifier

Milk Emulsions: Structure and Stability

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