Analysis of Light Scattering Data on the Calcium Ion Sensitivity of Caseinate Solution Thermodynamics: Relationship to Emulsion Flocculation

Dickinson, Eric; Семенова, М.Г.; Belyakova, Larisa E.; Antipova, Anna S.; Il'in, Michael M.; Tsapkina, E. N.; Ritzoulis, Christos

doi:10.1006/jcis.2001.7480

Cited by 66 publications

(30 citation statements)

References 30 publications

(48 reference statements)

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“…Those results are combined here with re-analysis of the same data using Eqs. (11) and (26). Before doing so, however, it is useful to examine the implications of some of the standard assumptions when LS experiments are conducted.…”

Section: Experimental Virial Coefficients and Apparent Molecular mentioning

confidence: 99%

“…Correcting for additional factors such as Donnan equilibrium in deriving Eq. (26) or (30) is left to a future report, and instead Eq. (11) is recommended for use more generally.…”

Section: B Classical Analysis Vs Kb Analysismentioning

confidence: 99%

“…However, for large deviations, differences between the de novo equations (Eqs. (11)), (26), and (30)), and the classical expression (Eq. (27) with constant A m 2 ) become more evident.…”

Section: B Classical Analysis Vs Kb Analysismentioning

confidence: 99%

“…(27) or (B6)) and the new expressions (Eqs. (11), (26), and (30)), for aCgn, and each antibody. These values are normalized by the true protein molecular weight M 2 derived from amino acid analysis.…”

Section: B Classical Analysis Vs Kb Analysismentioning

confidence: 99%

“…[25][26][27] In some cases, only the sign of B 22 is considered important, as a negative (positive) B 22 corresponds to net attractive (repulsive) protein-protein interactions relative to an ideal solution. 9,10,28 More recent work highlights the importance of considering an equivalent hard-sphere (HS) or purely steric proteinprotein interaction (i.e., B H S 22 ) as a more appropriate reference point.…”

Section: Introductionmentioning

confidence: 99%

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Reexamining protein–protein and protein–solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions

Blanco¹,

Şahin²,

Li³

et al. 2011

The Journal of Chemical Physics

203

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The classic analysis of Rayleigh light scattering (LS) is re-examined for multi-component protein solutions, within the context of Kirkwood-Buff (KB) theory as well as a more generalized canonical treatment. Significant differences arise when traditional treatments that approximate constant pressure and neglect concentration fluctuations in one or more (co)solvent/co-solute species are compared with more rigorous treatments at constant volume and with all species free to fluctuate. For dilute solutions, it is shown that LS can be used to rigorously and unambiguously obtain values for the osmotic second virial coefficient (B 22 ), in contrast with recent arguments regarding protein interactions deduced from LS experiments. For more concentrated solutions, it is shown that conventional analysis over(under)-estimates the magnitude of B 22 for significantly repulsive(attractive) conditions, and that protein-protein KB integrals (G 22 ) are the more relevant quantity obtainable from LS. Published data for α-chymotrypsinogen A and a series of monoclonal antibodies at different pH and salt concentrations are re-analyzed using traditional and new treatments. The results illustrate that while traditional analysis may be sufficient if one is interested in only the sign of B 22 or G 22 , the quantitative values can be significantly in error. A simple approach is illustrated for determining whether protein concentration (c 2 ) is sufficiently dilute for B 22 to apply, and for correcting B 22 values from traditional LS regression at higher c 2 values. The apparent molecular weight M 2,app obtained from LS is shown to generally not be equal to the true molecular weight, with the differences arising from a combination of protein-solute and protein-cosolute interactions that may, in principle, also be determined from LS.

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Section: Experimental Virial Coefficients and Apparent Molecular mentioning

confidence: 99%

“…Correcting for additional factors such as Donnan equilibrium in deriving Eq. (26) or (30) is left to a future report, and instead Eq. (11) is recommended for use more generally.…”

Section: B Classical Analysis Vs Kb Analysismentioning

confidence: 99%

“…However, for large deviations, differences between the de novo equations (Eqs. (11)), (26), and (30)), and the classical expression (Eq. (27) with constant A m 2 ) become more evident.…”

Section: B Classical Analysis Vs Kb Analysismentioning

confidence: 99%

Section: B Classical Analysis Vs Kb Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Reexamining protein–protein and protein–solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions

Blanco¹,

Şahin²,

Li³

et al. 2011

The Journal of Chemical Physics

203

View full text Add to dashboard Cite

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Nanotechnology in Food Production

Boom

2011

Nanotechnology in the Agri‐Food Sector

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Spontaneous Assembly and Induced Aggregation of Food Proteins

Bouhallab

Croguennec

2013

Advances in Polymer Science

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Beyond their nutritional value, food proteins are a versatile group of biopolymers with a considerable number of functionalities throughout their extensive structures, conformations and interaction–aggregation behaviour in solution. In the present paper, we give an overview of the induced aggregation and spontaneous reversible assembly of food proteins that lead to a diversity of supramolecular structures. After a brief description of the properties of some food proteins, the first part summarises the aggregation processes that lead to supramolecular structures with a variety of morphologies and sizes. The second part reports on the requirements that drive spontaneous assembly of oppositely charged proteins into reversible supramolecular structures. The promising new applications of these structures in food and non-food sectors are also mentioned

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Analysis of Light Scattering Data on the Calcium Ion Sensitivity of Caseinate Solution Thermodynamics: Relationship to Emulsion Flocculation

Cited by 66 publications

References 30 publications

Reexamining protein–protein and protein–solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions

Reexamining protein–protein and protein–solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions

Nanotechnology in Food Production

Spontaneous Assembly and Induced Aggregation of Food Proteins

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