Journal ArticleDOI
Complex Coacervation of Whey Proteins and Gum Arabic
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TLDR
A strong similarity is seen between the behavior of this system and a colloidal gas-liquid phase separation, and a "metastable" region delimited by a percolation line is seen.About:
This article is published in Biomacromolecules.The article was published on 2003-01-30. It has received 552 citations till now. The article focuses on the topics: Whey protein isolate & Whey protein.read more
Citations
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Application of response surface methodology and spectroscopic approach for investigating of curcumin nanoencapsulation using natural biopolymers and nonionic surfactant.
TL;DR: Biopolymer nanoparticles were assembled from sodium caseinate and gum arabic using electrostatic complexation in the presence of nonionic surfactant Tween 20 to investigate the interactions of curcumin with protein, polysaccharide and Surfactant.
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Driving force and pathway in polyelectrolyte complex coacervation
Shensheng Chen,Zhen-Gang Wang +1 more
TL;DR: In this paper , the temperature dependence in the dielectric constant of water can be exploited to extract the solvent entropy contribution in the electrostatic interactions, thereby resolving a major discrepancy between experiments and coarse-grained model studies concerning the thermodynamic driving force (i.e., entropy vs. energy) for polyelectrolyte complex coacervation.
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Generality and specificity of the binding behaviour of lysozyme with pectin varying in local charge density and overall charge
Yurij A. Antonov,Irina L. Zhuravleva,Miete Celus,Clare Kyomugasho,Salvatore Lombardo,Wim Thielemans,Marc Hendrickx,Paula Moldenaers,Ruth Cardinaels +8 more
TL;DR: In this article, the authors examined the similarities and differences of the binding behavior of lysozyme (lys) with pectin varying in local charge density and similar degree of methoxylation (DM).
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Deciphering the interactions of fish gelatine and hyaluronic acid in aqueous solutions.
TL;DR: The interactions of fish gelatine with hyaluronic acid are studied in an aqueous environment at 25°C by turbidimetric titration, confocal scanning laser microscopy, dynamic light scattering, zeta potentiometry, spectrophotometry with methylene blue, and construction of state diagrams.
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Alginate Trisaccharide Binding Sites on the Surface of β-Lactoglobulin Identified by NMR Spectroscopy: Implications for Molecular Network Formation.
Emil G. P. Stender,Johnny Birch,Christian Kjeldsen,Lau Dalby Nielsen,Jens Ø. Duus,Birthe B. Kragelund,Birte Svensson +6 more
TL;DR: A pH-dependent mechanism whereby both the BLGA dimer–monomer equilibrium and electrostatic interactions are exploited is suggested, which allows for control of coacervation and particle formation of BLGA/alginate mixtures via directed polysaccharide bridging of AOS binding sites and has implication for molecular network formation.
References
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Structure and Technofunctional Properties of Protein-Polysaccharide Complexes: A Review
TL;DR: The protein-polysaccharide complexes exhibit better functional properties than that of the proteins and polysaccharides alone, and could be attributed to the simultaneous presence of the two biopolymers, as well as the structure of the complexes.
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Protein–polysaccharide interactions
TL;DR: In this article, the authors describe the structure formation in the mixed systems in combination with rheological characterisation and make progress in the description of the mechanisms underlying the phase separation processes by the use of scattering techniques.
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Phase separation in polyelectrolyte solutions. Theory of complex coacervation
J. T. G. Overbeek,M. J. Voorn +1 more
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Polysaccharide protein interactions
C. G. de Kruif,Remco Tuinier +1 more
TL;DR: In this article, the interaction between proteins and polysaccharides, as can be observed in food related systems, is systematically discussed by separating biopolymer interactions into respectively enthalpy- and entropy-dominated types.
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Stability and rheological implications of electrostatic milk protein--polysaccharide interactions.
TL;DR: In this article, the authors studied the factors affecting the nature and strength of electrostatic protein-polysaccharide interactions and proposed a method to predict how solution conditions such as pH and ionic strength influence food macromolecular functional properties.