Thermodynamische Aspekte der Verträglichkeit von Eiweißen und Polysacchariden in wäßrigen Medien. 3. Mitt. Einige physikalisch‐chemische Faktoren des Phänomens der thermodynamischen Unverträglichkeit der Eiweiße und Polysaccharide

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

doi:10.1002/food.19790230902

Cited by 13 publications

(4 citation statements)

References 16 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: 98%

“…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%

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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: 98%

Section: Introductionmentioning

confidence: 99%

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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“…Proteins and acidic carboxyl-containing polysaccharides are known to have a limited compatibility within a broad range of pH values [6,[8][9][10][19][20][21]. At relatively high protein concentrations ( 2 6 %,) and low concentrations of acidic carboxyl-containing polysaccharide ( N 0.3 %,) the systems are two-phase.…”

Section: Discussionmentioning

confidence: 99%

Solubility of protein fibers obtained from casein solutions and liquid two‐phase water‐casein‐sodium alginate systems

Antonovcan

Zhuravskaya

Tolstoguzov

1985

Nahrung

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The solubility of protein and protein-polysaccharide matrix fibers obtained from casein solutions and two-phase water-casein-sodium alginate (W-C-A) systems in water and in 1 M NaCl solutions at different pH at 20 and 100 degrees C has been studied. The matrix fibers obtained from the two-phase W-C-A system are shown to be considerably less soluble than those from the casein solutions. This difference is seen particularly clearly when pH amounts to 5-7. However, it disappears with the spinning two-phase system at temperature above 80 degrees C. An assumption has been made about the matrix fibers being either mixed gels of the thermo-reversible, soluble calcium caseinate and thermo-irreversible insoluble calcium alginate, or complex protein-polysaccharide gels formed with the participation of the calcium ions. This latter assumption is in conformity with the negligible solubility of the protein fibers obtained as a result of the lyotropic gelation of the skimmed milk proteins.

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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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Thermodynamische Aspekte der Verträglichkeit von Eiweißen und Polysacchariden in wäßrigen Medien. 3. Mitt. Einige physikalisch‐chemische Faktoren des Phänomens der thermodynamischen Unverträglichkeit der Eiweiße und Polysaccharide

Cited by 13 publications

References 16 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

Solubility of protein fibers obtained from casein solutions and liquid two‐phase water‐casein‐sodium alginate systems

Interfacial tension of aqueous biopolymer mixtures close to the critical point

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