Thermodynamic incompatibility of the 11S fraction of soybean globulin and pectinate in aqueous medium

Семенова, М.Г.; Bolotina, V.S.; Grinberg, V. Ya.; Tolstoguzov, V. B.

doi:10.1016/s0268-005x(09)80222-1

Cited by 21 publications

(4 citation statements)

References 16 publications

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“…The quantitative thermodynamic analysis of the character of proteinepolysaccharide interactions may be carried out through the value of the cross second virial coefficient (A 23 ) (Antipova & Semenova, 1995;Semenova, 1996; Semenova, Bolotina, Grinberg, & Tolstoguzov, 1990;Semenova & Savilova, 1998), which is directly related to the chemical potentials of each component in the mixed system at constant pressure and temperature. A positive value of the cross second virial coefficient is a characteristic of the thermodynamically unfavourable (repulsive) interactions between unlike biopolymers that lead to the rise in the magnitudes of their chemical potentials, i.e., to the increase in their thermodynamic activities in the mixed solutions.…”

Section: Consequences Of Mixing Proteins and Polysaccharidesmentioning

confidence: 99%

Protein–polysaccharide interactions at fluid interfaces

2011

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Section: Consequences Of Mixing Proteins and Polysaccharidesmentioning

confidence: 99%

Protein–polysaccharide interactions at fluid interfaces

2011

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“…The phase behaviour of biopolymer mixtures can be predicted from the excluded volume of the macromolecules [10–12]. Because molecules are not penetrable by each other, a minimal distance between two spherical molecules of a globular protein equals the sum of their radii or the diameter of one of them.…”

Section: Incompatibility Of Biopolymers Excluded Volume Phase Diagramsmentioning

confidence: 99%

Origins of globular structure in proteins

Tolstoguzov

1999

FEBS Letters

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Thermodynamic incompatibility of polymers in a common solvent is possibly a driving force for formation and evolution of globular protein structures. Folding of polypeptide chains leads to a decrease in both excluded volume of molecules and chemical differences between surfaces of globular molecules with chemical information hidden in the hydrophobic interior. Folding of polypeptide chains results in`molecular or thermodynamic mimicry' of globular proteins and in at least more than 10-fold higher phase separation threshold values of mixed protein solutions compared to those of classical polymers. Unusually high co-solubility might be necessary for efficient biological functioning of proteins, e.g. enzymes, enzyme inhibitors, etc.z 1999 Federation of European Biochemical Societies.

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“…Discussing the thermodynamic compatibility of proteins and polysaccharides it is necessary to consider the second virial coefficients A pr-ps ("pr" for protein and "ps" for polysaccharide) of the interactions of both components on the one hand and A pr-pr and A ps-ps of the self-associations of the single components on the other hand [1][2][3][4]. For incompatible systems is (A pr-ps ) 2 A A pr-pr A ps-ps .…”

Section: Introductionmentioning

confidence: 99%

“…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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Thermodynamic incompatibility of the 11S fraction of soybean globulin and pectinate in aqueous medium

Cited by 21 publications

References 16 publications

Protein–polysaccharide interactions at fluid interfaces

Protein–polysaccharide interactions at fluid interfaces

Origins of globular structure in proteins

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

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