Food Proteins
Use Cases
Are the emulsifying properties of quinoa protein concentrates satisfactory for applications in the food industry ?
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Reference: Interfacial and Emulsifying Properties of Quinoa Protein Concentrates. M. L. López-Castejón; C. Bengoechea; J. Díaz-Franco; C. Carrera; Food Biophysics; doi.org/10.1007/s11483-019-09603-0.
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Quinoa is gaining more and more interest in the food industry. In this paper, the emulsification properties of two quinoa extracts, Q9 and Q 11 are studied.
The first step consisted in characterizing the interfacial properties of Q9 and Q11 at an oil water interface. Surface tension interfacial rheology measurement are carried out using a drop tensiometer (TRACKER™) . Then, the characterization of the emulsion system shows that Q11 has a higher emulsification capacity which is attributed to its better rheological properties. This finding highlights the correlation between the interfacial properties and the properties at the emulsion scale (emulsification and stability).
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TECLIS product: TRACKER™ automatic drop tensiometer
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Key words: Quinoa, protein, interfacial tension, interfacial rheology, emulsion, stability
How are the foam ability of ovalbumin proteins and the stability of foam containing ovalbumin affected by temperature ?
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Reference: Interfacial and Emulsifying Properties of Quinoa Protein Concentrates. R. J.B.M. Delahaije; F. J. Lech; P. A. Wierenga; Food Hydrocolloids 91 (2019) 263-274
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The effect of temperature on the formation and stabilization of ovalbumin foams is investigated. Specifically, the adsorption kinetics is characterized through surface pressure and elastic modulus measurements using a drop tensiometer (TRACKER™) at different temperatures (15 to 60°C) and, at the foam scale, the foam ability of ovalbumin is quantified by looking at the initial volume and bubble radius using a foam analyzer (FOAMSCAN™) and the Cell Size Analysis software.
It is found that increasing temperature results in a clear increase in adsorption kinetics and hence in an increase foam ability. However, increasing the temperature decreases the stability of ovalbumin stabilized foams which, ultimately, counters the increased foam ability.
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TECLIS product: TRACKER™ automatic drop tensiometer, FOAMSCAN™ foam analyzer, Cell Size Analysis software
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Key words: Protein, concentration, structural characterization, interfacial properties, adsorption rate, viscosity, foam ability, foam stability
What is the effect of the addition of low-molecular-weight surfactants on the stability of protein foams ?
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Reference: Identifying changes in chemical, interfacial and foam properties of β-lactoglobulin–sodium dodecyl sulphate mixtures. F. J. Lech; P. Steltenpool; M. B.J. Meinders; S. Sforza; H. Gruppenb; P. A. Wierenga; Colloids and Surfaces A: Physicochem. Eng. Aspects 462 (2014) 34–44
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The effect of the addition of SDS on the stability of β-lactoglobulin (BLG) foams is investigated. At the scale of the foam, the stability is characterized with a FOAMSCAN™ foam analyzer by measuring the foam half time t_(1⁄2). The foam stability reaches a minimum at a critical molar ratio MR=20 (SDS to BLG) then increases similarly to pure SDS. An analysis of the structure of the foam with the Cell Size Analysis software shows that this loss stability at the critical MR value is also represented by a sudden increase in mean bubble radius but, no correlation is observed between the foaming properties and the interfacial properties that are characterized in terms of surface pressure and dilatational modulus using a drop tensiometer (TRACKER™ by TECLIS). However, these experiments, at the scale of the interface, show that the interfacial composition is changing from a protein or protein–surfactant covered interface towards an interface covered solely by surfactants suggesting a protein-surfactant interaction. These findings are finally confirmed by surface tension measurements with a bulk exchange.
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TECLIS product: TRACKER™ automatic drop tensiometer with Bulk Exchange option, FOAMSCAN™ foam analyzer, Cell Size Analysis software
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Key words: Protein, foam stability, 2D rheology, protein-surfactant mixture, protein surfactant complexation
What are the physicochemical properties of rice protein ingredients and how do they compare to dairy protein ingredients ?
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Reference: Characterization of the physicochemical properties of intact and hydrolyzed rice protein ingredients. L. Amagliania; J. O'Reganb; C. Schmitt; A. L. Kellya; J. A. O'Mahony; Journal of Cereal Science 88 (2019) 16–23.
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The physico-chemical properties of different rice protein ingredients are probed and compared to dairy protein ingredients commonly used. First, intact rice protein ingredients are found to be moderately soluble in water while hydrolyzed rice protein ingredients show a higher solubility. In particular, rice endosperm protein hydrolysates (RPH) stand out thanks to their high solubility in water and their excellent foaming properties. Experiments at the scale of the foam using a FOAMSCAN™ foam analyzer show indeed that RPH show excellent foaming properties (foam capacity and foam stability).
Finally , RPH exhibits a very good heat stability which makes it a very good candidate as functional and value-added ingredient in a range of food product.
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TECLIS product: FOAMSCAN™ foam analyzer, Cell Size Analysis software
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Key words: Rice proteins, dairy proteins, foaming properties, heat stability , solubility
What are the contributions of long fibrils and peptides in the foaming behavior
of soy protein fibril systems ?
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Reference: Contribution of Long Fibrils and Peptides to Surface and Foaming Behavior of Soy Protein Fibril System. Z. Wan; X. Yang; L. M. C. Sagis; Langmuir 2016, 32, 8092−8101.
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Protein adsorption at the interfaces plays a major role in the stabilization of multiphase systems such as foams. In this paper the foaming properties of soy glycinin (11s) are investigated and the effect of heating, which results in the formation of fibrils and small peptides, is probed. The interfacial properties of pure peptides, pure fibrils and the mixture are first characterized by drop shape analysis tensiometry and surface dilational rheology experiments. The results shown that the interfacial behavior is mainly dominated by the peptides. The foaming properties of the three systems (peptides, fibrils and mixture) are then compared using a FOAMSCAN™ foam analyzer at different pH values. The analysis of the structure of the foam with the Cell Size Analysis software and the stability characterization with the foam half time show again that the foaming properties of the mixture are dominated by the small peptides. Finally, solution at high pH values seem to have better foaming properties. This is attributed to the formation of fibril clusters and peptide aggregates at these pH values.
TECLIS product: FOAMSCAN™ foam analyzer, Cell Size Analysis software
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Key words: Soy protein, drop tensiometry, interfacial rheology, foam stability
What is the impact of protein−surfactant interaction on the interfacial and foaming properties of a soy solution?
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Reference: Nonlinear Surface Dilatational Rheology and Foaming Behavior of Protein and Protein Fibrillar Aggregates in the Presence of Natural Surfactant. Z. Wan; X. Yang; L. M. C. Sagis; Langmuir 2016, 32, 3679-3690.
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The interfacial and the foaming properties of native soy glycinin (11S) are probed in the presence of the natural surfactant steviol glycoside (STE) before and after heat treatment. The interfacial properties are first characterized with a drop tensiometer and large-amplitude oscillatory dilatational rheology experiments. Compared to native 11S, the 11S fibril−peptide system showed faster adsorption kinetics. The adsorption properties of 11S were significantly affected by STE, most likely due to hydrophobic binding of 11S with STE. However, the results suggest that the peptide materials or fibrils resulting from the heat treatment do not interact with STE. At the scale of the foam, the foamability and the stability are characterized with a FOAMSCAN™ foam analyzer and the Cell Size Analysis software. No effect of STE is observed on the stability of 11S solutions unlike the fibril−peptide system where the foam stability is significantly reduced by STE. Finally, foams produced from the 11S fibril−peptide system were considerably more stable than those prepared from native 11S.
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TECLIS product: FOAMSCAN™ foam analyzer, Cell Size Analysis software
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Key words: Soy protein, heat treatment, protein-surfactant interaction, foamability, foam stability, interfacial rheology
What are the properties of oil-water
and air-water interfaces containing
plant-dairy protein blends ?
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Reference: Hinderink, Emma, et al. "Behavior of plant-dairy protein blends at air-water and oil-water interfaces." Colloids and Surfaces B: Biointerfaces (2020): 111015.
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The interfacial properties of oil-water and air-water interfaces containing plant-dairy proteins are probed through drop tensiometry measurements. Pea protein isolate (PPI) is used as a legume protein while two dairy proteins are used: whey protein isolate (WPI) and sodium caseinate (SC). Surface tension and oscillatory viscoelasticity measurements have been performed at different blend ratios. The results showed that, in general, higher elastic moduli and more rigid interfacial layers were formed at the air-water interface, compared to the oil-water interface, except for PPI.
TECLIS product: TRACKER™ automatic drop tensiometer
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Key words: plant-dairy blends, pea protein isolate, whey protein isolate, sodium caseinate, surface pressure, viscoelasticity, sunflower oil