Conformational state and charge determine the interfacial film formation and film stability of β-lactoglobulin

Kieserling, Helena; Pankow, Annika; Keppler, Julia K.; Wagemans, Anja Maria; Drusch, Stephan

doi:10.1016/j.foodhyd.2020.106561

Cited by 22 publications

(3 citation statements)

References 82 publications

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“…Therefore, it follows from Equation (14) that this effect is accounted for by the interaction parameter a and the derivative dlnω/dlnΓ (Figure 4b). The observed pH-induced variations of the latter quantity reflect the intermolecular interactions and the resulting molecular packing as affected by the protein net charge [85,86].…”

Section: 100 At ω*mentioning

confidence: 99%

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β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH

Gochev

Kovalchuk

Aksenenko

et al. 2021

Colloids and Interfaces

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The theoretical description of the adsorption of proteins at liquid/fluid interfaces suffers from the inapplicability of classical formalisms, which soundly calls for the development of more complicated adsorption models. A Frumkin-type thermodynamic 2-d solution model that accounts for nonidealities of interface enthalpy and entropy was proposed about two decades ago and has been continuously developed in the course of comparisons with experimental data. In a previous paper we investigated the adsorption of the globular protein β-lactoglobulin at the water/air interface and used such a model to analyze the experimental isotherms of the surface pressure, Π(c), and the frequency-, f-, dependent surface dilational viscoelasticity modulus, E(c)f, in a wide range of protein concentrations, c, and at pH 7. However, the best fit between theory and experiment proposed in that paper appeared incompatible with new data on the surface excess, Γ, obtained from direct measurements with neutron reflectometry. Therefore, in this work, the same model is simultaneously applied to a larger set of experimental dependences, e.g., Π(c), Γ(c), E(Π)f, etc., with E-values measured strictly in the linear viscoelasticity regime. Despite this ambitious complication, a best global fit was elaborated using a single set of parameter values, which well describes all experimental dependencies, thus corroborating the validity of the chosen thermodynamic model. Furthermore, we applied the model in the same manner to experimental results obtained at pH 3 and pH 5 in order to explain the well-pronounced effect of pH on the interfacial behavior of β-lactoglobulin. The results revealed that the propensity of β-lactoglobulin globules to unfold upon adsorption and stretch at the interface decreases in the order pH 3 > pH 7 > pH 5, i.e., with decreasing protein net charge. Finally, we discuss advantages and limitations in the current state of the model.

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Section: 100 At ω*mentioning

confidence: 99%

“…The precritical regions of the data sets at different pH are localized along the c-axis in the same way as in the isotherms of the surface pressure Π(c) and the surface excess Γ(c) (Figure 1) that follows from the theory. [85,86].…”

Section: Experimental and Computed Dependencies E(π)fg And E(γ)fg Amentioning

confidence: 99%

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH

Gochev

Kovalchuk

Aksenenko

et al. 2021

Colloids and Interfaces

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show abstract

“…The protein layer at the oil–water interface is in a dynamic equilibrium which could be affected by the structure and intermolecular interaction of proteins [ 27 ]. The protein layer will undergo reversible collapse when the amount of protein exceeds the maximum molecule density, and the reform of the interfacial membrane was driven by the attraction force of protein at the oil–water interface [ 28 ]. The peppermint oil emulsions with 2% proteins were not analyzed, since they separated into the creaming layer and the aqueous phase upon preparation with SC and after 2 days with WPI and hWPI.…”

Section: Resultsmentioning

confidence: 99%

Effect of Oil Type on Spatial Partition of Resveratrol in the Aqueous Phase, the Protein Interface and the Oil Phase of O/W Emulsions Stabilized by Whey Protein and Caseinate

2023

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Oil-in-water emulsions contain the inner oil phase, the protein membrane at the interface and the aqueous phase. In this study, the spatial partition of resveratrol was investigated in sunflower oil, fish oil, medium-chain triglyceride (MCT) and peppermint oil emulsions stabilized by native whey protein isolate (WPI), heat-denatured WPI and sodium caseinate. Resveratrol was added in the aqueous phase of emulsions and its partition was analyzed in term of resveratrol solubility in bulk oil and in the aqueous phase of protein, protein concentration and interfacial protein. The final concentrations of resveratrol in the aqueous phase were basically greater than those in the oil phase of fish oil, sunflower oil and MCT oil emulsions, while the final concentrations of resveratrol in the oil phase were greater than those in the aqueous phase of peppermint oil emulsions. The difference in the interfacial partition of resveratrol and proteins increased as the polyphenol solubility in bulk oil increased. Resveratrol solubility in the oil phase drove its transfer from the aqueous phase into the oil phase in all emulsions, except that the interfacial protein also contributed to the transfer in fish oil emulsions. The oil–water interface provided the microenvironment for the enrichment of resveratrol by proteins.

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Mechanisms of stabilization of proteins by surfactants

Khan,

Gomes,

Grapentin

et al. 2023

Surfactants in Biopharmaceutical Development

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Conformational state and charge determine the interfacial film formation and film stability of β-lactoglobulin

Cited by 22 publications

References 82 publications

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH

β-Lactoglobulin Adsorption Layers at the Water/Air Surface: 5. Adsorption Isotherm and Equation of State Revisited, Impact of pH

Effect of Oil Type on Spatial Partition of Resveratrol in the Aqueous Phase, the Protein Interface and the Oil Phase of O/W Emulsions Stabilized by Whey Protein and Caseinate

Mechanisms of stabilization of proteins by surfactants

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