Thermodynamische Aspekte der Verträglichkeit von Eiweißen und Polysacchariden in wäßrigen Medien. 2. Mitt. Phänomenologie der thermodynamischen Unverträglichkeit von Eiweißen und Polysacchariden in wäßrigen Medien

Antonov, Ju. A.; Grinberg, V. Ja.; Tolstoguzov, V. B.

doi:10.1002/food.19790230605

Cited by 21 publications

(12 citation statements)

References 2 publications

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“…That the formation of weak complexes between protein and PS results in a singlephase state of these systems was shown previously. [22][23][24]28,52,53 The nature of the forces stabilizing these complexes is not known. Hydrogen bonding between chain segments belonging to polymer 1 and polymer 2 has been suggested to interpret the miscibility observed for a few polymer pairs in aqueous solvents, 5 but this hypothesis does not seem to be able to explain the effects of pH and ionic strength on the compatibility of casein-guar systems we have described.…”

Section: Discussion and Concluding Remarksmentioning

confidence: 99%

“…21 Thermodynamic incompatibility between PSs and proteins shows itself only when the possibility of intermacromolecular complexes formation is excluded. [22][23][24] Although the majority of biopolymer mixtures show phase separation, those containing two linear anionic PSs remain single phase. The other systems, including mixtures of both charged and neutral PSs, as well as linear anionic PS-gelatin systems, were two-phase only at an ionic strength Ͼ0.09 -0.2.…”

Section: Introductionmentioning

confidence: 99%

“…where subscripts 1, 2, and 3 relate to the solvent, the protein, and the PS, respectively; K ϭ 2 Experimental errors are 12% on A 12 and A 13 , and 30% on A 23 .…”

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confidence: 99%

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On the one‐phase state of aqueous protein‐uncharged polymer systems: Casein‐guar gum system

Antonov

Jacques

Doublier

1999

J. Appl. Polym. Sci.

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ABSTRACT:Although the majority of biopolymers are incompatible in water, systems containing casein molecules and a neutral polysaccharide (guar gum galactomannan) showed phase separation only at an ionic strength above 0.09 -0.2. Static light scattering, circular dichroism spectroscopy, velocity sedimentation, viscosimetry, phase analysis in different solvents, and Rosenberg's method were used to estimate the effect of polymer-solvent and polymer-polymer interactions on the phase state of casein-guar aqueous systems. Different solvent conditions were used to try to clarify the nature (electrostatic or nonelectrostatic) of the interaction between the two macromolecular species. Data obtained show that the dominant mechanism controlling the single-phase state at low ionic strength (below 0.01) involves the formation of water-soluble weak interpolymer complexes, which may be destroyed by increasing ionic strength.

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Section: Discussion and Concluding Remarksmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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On the one‐phase state of aqueous protein‐uncharged polymer systems: Casein‐guar gum system

Antonov

Jacques

Doublier

1999

J. Appl. Polym. Sci.

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“…The caseinate at neutral pH is thus negatively charged, like alginate. Both biopolymers are well known, widely used in industry, and the thermodynamic behaviour of the ternary water-caseinate-alginate systems is known from literature [6,[25][26][27][28].…”

Section: Methodsmentioning

confidence: 99%

Interfacial tension of aqueous biopolymer mixtures close to the critical point

Antonov¹,

Puyvelde²,

Moldenaers³

2004

International Journal of Biological Macromolecules

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Proteins and polysaccharides, being the main constructional materials in many biological structures, have a limited compatibility in aqueous media. At sufficiently high concentrations, they form water-in-water emulsions. Interfacial tension is an important parameter in such systems since it is a controlling factor in the morphology development during processing. In this work a rheo-optical methodology, based on the analysis of small angle light scattering (SALS) patterns during fibril break-up, is used to study the interfacial tension of water-sodium caseinate-sodium alginate systems located close to and relatively far from the binodal. The interfacial tension close to the critical point was ∼10 −8 N/m, and it increased considerably, to a value of up to 5.2 × 10 −6 N/m farther from the critical point. For the scaling of the interfacial tension with the density difference between the phases, a scaling exponent of 3.1 ± 0.3 was found, in agreement with the critical mean-field scaling exponent of 3.

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“…Pectins were tested for their compatibility with different proteins, such as blood serum albumins, egg, milk and soy proteins in liquid systems [2,3,[5][6][7][8] and also in gels [9,10]. The influence of the pectin structure on the thermodynamic compatibility with proteins was examined by Semenova et al [11], using human serum albumin and by Antonov et al [12] using gelatine.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamic compatibility of sodium caseinate with different pectins. Influence of the milieu conditions and pectin modifications

Einhorn-Stoll¹,

Salazar

Jaafar

et al. 2001

Nahrung

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Combinations of pectins and caseins are ingredients of many food products. Therefore the thermodynamic compatibility of both components was examined to investigate the influences of environmental factors as well as of the structure of the pectin. High-methoxyl pectin was demethoxylated and amidated, respectively, and tested for the compatibility with sodium caseinate under varying conditions of pH and ionic strength. The compatibility increased with increasing pH and decreasing ionic strength. Demethoxylated pectins were more and amidated pectins less compatible with the caseinate. Changes in the pectin hydrophilicity, solubility and molecular weight and possibly local interactions such as electrostatic attraction, hydrogen bonding and calcium bridges are involved in the compatibility of the components. The type and degree of the pectin modifications as well as the type, composition and properties of the protein were found to be of great importance for the thermodynamic compatibility.

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Thermodynamische Aspekte der Verträglichkeit von Eiweißen und Polysacchariden in wäßrigen Medien. 2. Mitt. Phänomenologie der thermodynamischen Unverträglichkeit von Eiweißen und Polysacchariden in wäßrigen Medien

Cited by 21 publications

References 2 publications

On the one‐phase state of aqueous protein‐uncharged polymer systems: Casein‐guar gum system

On the one‐phase state of aqueous protein‐uncharged polymer systems: Casein‐guar gum system

Interfacial tension of aqueous biopolymer mixtures close to the critical point

Thermodynamic compatibility of sodium caseinate with different pectins. Influence of the milieu conditions and pectin modifications

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