Journal Article10.1111/J.1432-1033.1994.00883.X
A model for the denaturation and aggregation of beta-lactoglobulin.
TL;DR: A quantitatively correct kinetic model for the temperature-induced denaturation and aggregation of beta-lactoglobulin is presented and recognizes an initiation, a propagation and a termination step by analogy with polymer radical chemistry.
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Abstract: A quantitatively correct kinetic model for the temperature-induced denaturation and aggregation of beta-lactoglobulin is presented. The model recognizes an initiation, a propagation and a termination step by analogy with polymer radical chemistry. The decrease in native beta-lactoglobulin is predicted to follow order 3/2, in agreement with experimental results. The size of the protein polymer particles is predicted to be proportional to the square root of the initial beta-lactoglobulin concentration. The scattered light intensity is proportional to the product of concentration and size of the protein polymer particles. The initial increase in scattering intensity of the particles therefore scales with the initial squared beta-lactoglobulin concentration. The influence of other reaction conditions, e.g. ionic strength and pH, can be incorporated via the reaction constants of the reaction kinetic pathway.
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Citations
Acid-induced gelation of whey protein polymers: effects of pH and calcium concentration during polymerization
Michel Britten,Hélène J. Giroux +1 more
TL;DR: In this article, the effect of mineral environment during heating on the hydrodynamic characteristics and acid-induced gelation properties of polymers was studied, showing that polymers with high intrinsic viscosity produced stronger gels, suggesting a relationship between polymer shape and gel strength.
140
Structural and interaction properties of β-Lactoglobulin as studied by FTIR spectroscopy
Thierry Lefèvre,Muriel Subirade +1 more
TL;DR: In this paper, new aspects of β-Lactoglobulin (BLG) structure which have not previously been found by FT-IR spectroscopy are presented, related to the modifications of the quaternary structure of BLG, i.e. to the monomeric or dimeric forms.
137
Heat-induced interactions of β-lactoglobulin and α-lactalbumin with the casein micelle in pH-adjusted skim milk
TL;DR: In this paper, the authors measured the extent of β-lactoglobulin denaturation and their subsequent association with the casein micelle in skim milks, adjusted to pH 6.48, 6.60 or 6.83.
137
Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH
TL;DR: Heat-induced aggregation of β -lactoglobulin AB was studied using size-exclusion chromatography in combination with multi-angle laser light scattering and electrophoretic techniques so that the formation of irreversibly altered monomers and non-native dimers could be monitored.
130
Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate
TL;DR: In this article, the effect of heat treatment on the antigenicity of α-lactalbumin (α-LA) and β-Lactoglobulin (β-LG) in whey protein isolate (WPI) was investigated at temperatures in the range of 50-120°C for times from 0.5 to 30 min.
128
References
Principles of Polymer Chemistry.
TL;DR: A good introduction to the history of the POLYMER CHEMISTRY can be found in this paper, where the authors present a good overview of the history and history of their work.
15.1K
Light Scattering by Small Particles
H. C. Van de Hulst,V. Twersky +1 more
TL;DR: Light scattering by small particles as mentioned in this paper, Light scattering by Small Particle Scattering (LPS), Light scattering with small particles (LSC), Light Scattering by Small Parts (LSP),
10.4K
•Book
Light Scattering by Small Particles
H. C. van de Hulst
- 01 Dec 1981
TL;DR: Light scattering by small particles as mentioned in this paper, Light scattering by Small Particle Scattering (LPS), Light scattering with small particles (LSC), Light Scattering by Small Parts (LSP),
7.9K
The structure of β -lactoglobulin and its similarity to plasma retinol-binding protein
Miroslav Z. Papiz,Lindsay Sawyer,Elias Eliopoulos,Anthony C.T. North,John B. C. Findlay,R. Sivaprasadarao,T.A. Jones,M. E. Newcomer,P. J. Kraulis +8 more
TL;DR: A possible binding site for retinol in BLG has been identified by model-building and a role for BLG in vitamin A transport is suggested and specific receptors for the BLG–retinol complex in the intestine of neonate calves are discovered.
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