Protein oleogels from heat-set whey protein aggregates

Vries, Auke de; Wesseling, Anne; Linden, Erik van der; Scholten, Elke

doi:10.1016/j.jcis.2016.09.043

Cited by 94 publications

(47 citation statements)

References 43 publications

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“…1 In this procedure, the polarity of the solvent was changed gradually to remove the surrounding water from the WPI aggregates and replace the continuous phase for oil. In short, 15 g of aqueous pellet, containing the WPI aggregates, was redispersed in 150 mL of acetone, and mixed thoroughly using rotor stator homogenization.…”

Section: Methodsmentioning

confidence: 99%

“…To enhance the control over the network formation, we then prepared whey protein aggregates of colloidal size (∼150 nm) as initial building blocks. 1 In this Research Article, we showed that the solvent exchange procedure was able to prevent agglomeration of preformed heat-set aggregates and therefore enabled gel formation due to sufficient protein–protein interactions. Alternatively, when the protein aggregates were freeze-dried to remove the water before they were dispersed in oil, irreversible agglomeration of the initial particles was obtained.…”

Section: Introductionmentioning

confidence: 93%

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Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business

Vries

Gomez

Jansen

et al. 2017

ACS Appl. Mater. Interfaces

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Proteins are known to be effective building blocks when it comes to structure formation in aqueous environments. Recently, we have shown that submicron colloidal protein particles can also be used to provide structure to liquid oil and form so-called oleogels (de VriesA.de VriesA.27693552J. Colloid Interface Sci.20174867583. To prevent particle agglomeration, a solvent exchange procedure was used to transfer the aggregates from water to the oil phase. The aim of the current paper was to elucidate on the enhanced stability against agglomeration of heat-set whey protein isolate (WPI) aggregates to develop an alternative for the solvent exchange procedure. Protein aggregates were transferred from water to several solvents differing in polarity to investigate the effect on agglomeration and changes in protein composition. We show that after drying protein aggregates by evaporation from solvents with a low polarity (e.g., hexane), the protein powder shows good dispersibility in liquid oil compared to powders dried from solvents with a high polarity. This difference in dispersibility could not be related to changes in protein composition or conformation but was instead related to the reduction of attractive capillary forces between the protein aggregates during drying. Following another route, agglomeration was also prevented by applying high freezing rates prior to freeze-drying. The rheological properties of the oleogels prepared with such freeze-dried protein aggregates were shown to be similar to that of oleogels prepared using a solvent exchange procedure. This Research Article provides valuable insights in how to tune the drying process to control protein agglomeration to allow for subsequent structure formation of proteins in liquid oil.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business

Vries

Gomez

Jansen

et al. 2017

ACS Appl. Mater. Interfaces

Self Cite

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“…To prepare the protein oleogels, the WPI aggregates were transferred to the 4 different oil types using a solvent exchange procedure as described previously. 25 In this procedure, the polarity of the solvent was changed gradually to remove the surrounding water from the WPI aggregates and replace the continuous phase for oil. In short, 15 g of aqueous pellet, containing the WPI aggregates, was re-dispersed in 150 mL acetone, and mixed thoroughly using rotor stator homogenization at 13 000 rpm for 3 min.…”

Section: Oil Propertiesmentioning

confidence: 99%

The effect of oil type on network formation by protein aggregates into oleogels

et al. 2017

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The aim of this study was to assess the effect of oil type on the network formation of heat-set protein aggregates in liquid oil. The gelling properties of such aggregates to structure oil into so-called 'oleogels' are related to both the particle-particle and particle-solvent interactions. To change these interactions, four different oils (medium chain triglyceride oil, sunflower oil, extra virgin olive oil and castor oil) differing in polarity were used. The rheological properties of the protein aggregate oleogels were determined and compared to gels prepared with hydrophilic and hydrophobic colloidal silica particles at the same concentration. The results show that gel strength of the network formed by protein aggregates is affected by the polarity of the oil, resulting in weaker gels in more polar oils as a result of larger particle-solvent interactions. Similar results were obtained for hydrophilic silica particles. In the case of castor oil, the increased particle-solvent interactions though hydrogen bonds limited gel formation for all particle types. Large deformation rheology shows that protein oleogels exhibit a yielding behaviour under large deformation, but regenerate its elasticity quickly after deformation is reduced. The rapid recovery of the protein network and the fact that the interactions between the protein aggregates can be tuned by changing the characteristics of the oil, may be interesting features for various applications in foods.

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“…This paper focuses on whey protein as polymer for structuring the oil. These oleogels contain a high oil content and no heating step that includes the oil phase is needed . Thus, the aim of this study is the evaluation of the oxidative stability of a whey protein based oleogel during storage.…”

Section: Introductionmentioning

confidence: 99%

Influence of Water Addition on Lipid Oxidation in Protein Oleogels

Meissner

Keppler

Stöckmann

et al. 2019

Euro J Lipid Sci & Tech

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The aim of the present study is the investigation of lipid oxidation in protein based oleogels. For this purpose, oleogels are prepared by suspension of freeze dried whey protein isolate aggregates and small amounts of water (<10%) in purified oleic rich safflower oil. The formation of conjugated dienes positively correlates with the addition of water. In contrast, a lower concentration of aldehydes is measured by headspace gas chromatography in oleogels with higher water addition, indicating a water facilitated degradation of aldehydes reacting with proteins. Determination of water activity indicates the presence of water droplets at higher water addition to oleogels. Furthermore, changes in the surface appearance (greasy‐glossy to dull) and the texture (consistent gel vs. crumbly) structure are indicative of microstructural changes due to increased water addition. The study suggests that water droplet formation is responsible for the marked increase in lipid oxidation. However, cross reaction of aldehydes with proteins is suggested to result in lowering the levels of secondary lipid oxidation products hexanal and propanal in oleogel. Practical Applications: The practical applications of the present work are related to the fabrication, processing, storage and consumption of oleogels and other protein‐lipid‐matrices. The results clearly indicate oleogels are prone to oxidation and proteins are involved by cross‐reaction resulting in visible browning during storage. Oxidation products such as hexanal (marker for secondary lipid oxidation) may not reflect the level of oxidation due to degradation by cross‐reactions with proteins. The aim of the present study is the investigation of lipid oxidation in protein based oleogels. The formation of conjugated dienes positively correlates with the addition of water. In contrast, a lower concentration of aldehydes is measured in oleogels with higher water addition. Water activity indicates the presence of water droplets at higher water addition to oleogels, which are likely responsible for the marked increase in lipid oxidation. However, cross reaction of aldehydes with proteins is suggested to result in lowering the levels of secondary lipid oxidation products hexanal and propanal in oleogels.

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Protein oleogels from heat-set whey protein aggregates

Cited by 94 publications

References 43 publications

Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business

Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business

The effect of oil type on network formation by protein aggregates into oleogels

Influence of Water Addition on Lipid Oxidation in Protein Oleogels

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