Complex coacervation of β-lactoglobulin – κ-Carrageenan aqueous mixtures as affected by polysaccharide sonication

Hosseini, Seyed Mohammad Hashem; Emam‐Djomeh, Zahra; Razavi, Seyed Hadi; Moosavi-Movahedi, Ali Akbar; Saboury, Ali Akbar; Mohammadifar, Mohammad Amin; Farahnaky, Asgar; Atri, Maliheh Sadat; Meeren, Paul Van der

doi:10.1016/j.foodchem.2013.02.090

Cited by 76 publications

(35 citation statements)

References 27 publications

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“…ITC revealed that the binding between βLgA and pectin with DM less than the 86R was an exothermic process which was consistent with previously published results 12,15 . As reported by others the endothermic process at the end stage of the titration is due to dilution 14,16 . The titration features a sequence of strong exothermic peaks that gradually decrease in intensity until the exothermic peaks have become endothermic peaks of constant intensity.…”

Section: Resultsmentioning

confidence: 52%

“…Other interactions could include hydrophobic, hydrogen-bonding and steric interactions 10 . Interactions between proteins and polysaccharides depend on the type of polymer and the molar ratio of protein to polysaccharide as well as the state of the solution such as its pH, ionic strength and temperature 5, 11-13 . β-Lactoglobulin (βLg) has been used extensively as a model protein to study the interaction with a range of polysaccharides [14][15][16][17] . βLg is the major whey protein in the milk of ruminants and other mammals 18 .…”

Section: Introductionmentioning

confidence: 99%

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Structural mechanism of complex assemblies: characterisation of beta-lactoglobulin and pectin interactions

Melton

Jameson

et al. 2015

Soft Matter

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Knowledge of how proteins and polysaccharides interact is the key to understanding encapsulation and emulsification in these composite systems and ultimately to understanding the structures of many biological network systems. As a model system we have studied β-lactoglobulin A (βLgA) interacting with pectins of various amounts and distribution patterns of charge. The studies were conducted at pH 4 at minimal ionic strength, where the βLgA and the pectins are oppositely charged, resulting in an electrostatic attraction to each other. Isothermal titration calorimetry (ITC) experiments were performed to determine the thermodynamics associated with βLgA-pectin titration. It was found that βLgA only interacted with pectins with an adequate amount of charge, and that the complexation between βLgA and pectin was a two-step process initially involving binding of the protein to available sites on the pectin, and subsequently binding of the protein onto the bound protein that has previously adsorbed. Circular dichroism (CD) and intrinsic tryptophan fluorescence were also measured of βLgA during its interaction with the pectin samples, and show that the binding leads to significant conformational changes in βLgA. An increase in the turbidity of the solution of the resultant complexes indicates the formation of large-scale interpolymer associations of the primary complexes mediated by protein-rich domains.

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Section: Resultsmentioning

confidence: 52%

Section: Introductionmentioning

confidence: 99%

Structural mechanism of complex assemblies: characterisation of beta-lactoglobulin and pectin interactions

Melton

Jameson

et al. 2015

Soft Matter

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“…HOSSEINI et al (2013) submitted the κ-carrageenan biopolymer (KC) and β-LG on ultrasound, and reported that KC-BLG interactions were exothermic with negative and favorable enthalpy and negative and unfavorable entropy. A significant reduction in the affinity constant of the formation of complex coacervates suggested a conformational change.…”

Section: Isothermal Titration Calorimetry (Itc)mentioning

confidence: 99%

Calorimetric techniques applied to the thermodynamic study of interactions between proteins and polysaccharides

2016

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“…Therefore, these complexes have great potential as a bioresponsive material for controlled release [23**, 24,27,32] or in the reduction of salt, sugars or fats in foods, as the sensory perception of taste and flavour can be altered by tuning the microstructures [33][34][35]. Proteinpolysaccharide complexes have also been shown to exhibit "better" functional properties than proteins and polysaccharides alone, for example, hydration and interfacial properties [25].…”

Section: Polysaccharide -Protein Complexesmentioning

confidence: 99%

The parallel lives of polysaccharides in food and pharmaceutical formulations

Kontogiorgos¹,

Smith²,

Morris³

2015

Current Opinion in Food Science

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The present opinion article discusses how polysaccharide structures can be used in both food and pharmaceutical formulations. We distinguish two regions depending on moisture content where polysaccharides form structures with distinct functional properties. Some trends in key areas of active research are assessed and in particular edible films, encapsulation, polycrystalline polysaccharides, protein-polysaccharide coacervation and fluid gels. We unveil that the physicochemical principles that are shared across the food and pharmaceutical disciplines provide a great opportunity for crossdisciplinary collaboration. We finally argue that such co-operation will help tackling polysaccharide functionality issues that are encountered in both areas.3

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Complex coacervation of β-lactoglobulin – κ-Carrageenan aqueous mixtures as affected by polysaccharide sonication

Cited by 76 publications

References 27 publications

Structural mechanism of complex assemblies: characterisation of beta-lactoglobulin and pectin interactions

Structural mechanism of complex assemblies: characterisation of beta-lactoglobulin and pectin interactions

Calorimetric techniques applied to the thermodynamic study of interactions between proteins and polysaccharides

The parallel lives of polysaccharides in food and pharmaceutical formulations

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