Improved heat stability by whey protein–surfactant interaction

Le, T. Tran; Sabatino, Paolo; Heyman, Bart; Kasinos, M.; Dinh, Huy-Hong-Quan; Dewettinck, Koen; Martins, José; Meeren, Paul Van der

doi:10.1016/j.foodhyd.2010.07.012

Cited by 32 publications

(6 citation statements)

References 41 publications

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“…Though interactions between WP and surfactants may occur at room temperature, they can only be obviously observed during thermal treatment (Le et al, 2011). Thermal gelation properties of WP in the presence of soybean lecithin were monitored by an oscillation rheology and results were shown in Figure 5A.…”

Section: Oscillation Rheological Properties Of Wp or Pwp In The Presementioning

confidence: 99%

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

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Soybean lecithin is often used as a surfactant in food formulation. The aim of this study was to investigate the interactions between soybean lecithin (SL, 0-3%, wt/vol) and whey protein (WP, 10%, wt/vol) or polymerized whey protein (PWP, 10%, wt/vol) induced by heating WP solutions at 85°C for 0 to 20 min at pH 7.0. The samples were evaluated for zeta potential, particle size, morphology, rheological properties, thermal properties, secondary structure, and surface hydrophobicity. Zeta potential of WP increased linearly as SL level increased from 0 to 3%, whereas that of PWP changed with plateau at SL level of 1%, which may be due to the aggregation of SL. The addition of SL increased the particle size and apparent viscosity of both WP and PWP. All the samples exhibited different morphology depending on SL level and heating time according to transmission electron microscopy images. Whey protein showed obviously decreased gelation time and increased storage modulus in the presence of SL. Differential scanning calorimetry curves confirmed the effects of SL on the thermal properties of both WP and PWP. Circular dichroism spectra indicated that SL had effects on the secondary structure of both WP and PWP. The changes in surface hydrophobicity indicated the hydrophobic interactions between WP/PWP and SL. Data indicate that the physicochemical and functional properties of WP and PWP can be altered by adding soybean lecithin.

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Section: Oscillation Rheological Properties Of Wp or Pwp In The Presementioning

confidence: 99%

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Sun

Wang

Guo

2018

Journal of Dairy Science

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“…The increase in the aggregate size with the addition of these emulsifiers was not expected and is in contrast to observations reported before. Several studies observed a reduction in aggregate size when non-ionic emulsifiers were added to the protein before heating. , Hansted et al proposed the formation of emulsifier micelles with or around BLG and, thus, a solubilization of the protein, making it more difficult for the molecules to approach each other. However, there were differences regarding the systems used within the published studies and in this present work.…”

Section: Resultsmentioning

confidence: 99%

Properties of β-Lactoglobulin Aggregates and Gels as Affected by Ternary Emulsifier Mixtures of Tween 20, Lecithin, and Sucrose Palmitate

Wiedenmann

Frister

Oehlke

et al. 2019

J. Agric. Food Chem.

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The influence of sucrose palmitate, Tween 20, and lecithin on the properties of heat-induced aggregates and cold-set gels of β-lactoglobulin was studied based on an experimental mixture design with a fixed total emulsifier concentration. Emulsifiers were added to the protein solution before heating. Aggregate size and absolute values of ζ potential increased with the addition of emulsifiers, among which lecithin had the most pronounced effect. The water retention of the aggregates correlated positively with the aggregate size. Gels had reduced fracture stress and strains with increasing sucrose palmitate and decreasing Tween 20 contents. The fracture properties correlated with the ζ potentials of the aggregates, and larger aggregates led to gels with higher water-holding capacities. The emulsifiers hence influenced the gel properties indirectly via the aggregate properties. The impact of emulsifiers on food structures should therefore be considered when a food product is designed.

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“…Whey proteins are milk proteins (mainly β-lactoglobulin and α-lactalbumin) that are widely used in food design due to a variety of functionalities, including: water binding, gelation, emulsification, and foaming [ 77 ]. In food processing, whey proteins are usually denatured due to heat treatments and thereby they aggregate, either in self-aggregation or with other food particles [ 78 , 79 ]. Through extensive research, it has been shown that the interactions between whey proteins and small molecules can change their molecular structures and the physico-chemical properties [ 79 ], supporting their applications in food.…”

Section: Proteins In Milkmentioning

confidence: 99%

“…In food processing, whey proteins are usually denatured due to heat treatments and thereby they aggregate, either in self-aggregation or with other food particles [ 78 , 79 ]. Through extensive research, it has been shown that the interactions between whey proteins and small molecules can change their molecular structures and the physico-chemical properties [ 79 ], supporting their applications in food.…”

Section: Proteins In Milkmentioning

confidence: 99%

Roles of Proteins/Enzymes from Animal Sources in Food Quality and Function

Gan

et al. 2021

Foods

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Animal proteins are good sources of protein for human, due to the composition of necessary amino acids. The quality of food depends significantly on the properties of protein inside, especially the gelation, transportation, and antimicrobial properties. Interestingly, various kinds of molecules co-exist with proteins in foodstuff, and the interactions between these can significantly affect the food quality. In food processing, these interactions have been used to improve the texture, color, taste, and shelf-life of animal food by affecting the gelation, antioxidation, and antimicrobial properties of proteins. Meanwhile, the binding properties of proteins contributed to the nutritional properties of food. In this review, proteins in meat, milk, eggs, and fishery products have been summarized, and polysaccharides, polyphenols, and other functional molecules have been applied during food processing to improve the nutritional and sensory quality of food. Specific interactions between functional molecules and proteins based on the crystal structures will be highlighted with an aim to improve the food quality in the future.

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Improved heat stability by whey protein–surfactant interaction

Cited by 32 publications

References 41 publications

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Properties of β-Lactoglobulin Aggregates and Gels as Affected by Ternary Emulsifier Mixtures of Tween 20, Lecithin, and Sucrose Palmitate

Roles of Proteins/Enzymes from Animal Sources in Food Quality and Function

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