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
Influence of ι-Carrageenan on Droplet Flocculation of β-Lactoglobulin-Stabilized Oil-in-Water Emulsions during Thermal Processing
TL;DR: In this article, the influence of thermal processing on droplet flocculation in oil-in-water emulsions stabilized by either β-lactoglobulin (primary emulsion) or β-Lg−I-carrageenan (secondary emulsion), at pH 6 has been investigated.
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Comparative study on foaming and emulsifying properties of different beta-lactoglobulin aggregates
Jing Hu,Jing Hu,Jixin Yang,Yao Xu,Ke Zhang,Katsuyoshi Nishinari,Glyn O. Phillips,Yapeng Fang,Yapeng Fang +8 more
TL;DR: The foaming stability seemed to be more controlled by interfacial elasticity while the emulsion stability was more determined by surface charges, and AFM analysis demonstrated different microstructures at the air-water interface between pH 4.0 and 7.0.
Kinetics of rennet casein gelation at different cooling rates.
TL;DR: This study illustrated that structure formation resulted from the addition of flocs into the protein network: not allFlocs were part of the network at a defined gel point, so the structure and thus quality of dairy products may be better controlled.
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Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin
TL;DR: The antigenic response of β-lactoglobulin (β-Lg), treated by dynamic high-pressure microfluidization (DHPM) at different temperatures, was determined by an indirect competitive enzyme-linked immunosorbent assay using polyclonal antibodies from rabbit serum.
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Influence of the Maillard reaction on the properties of cold-set whey protein and maltodextrin binary gels
TL;DR: In this article, WPI was conjugated with maltodextrin through the Maillard reaction and used to form cold-set gels, which increased gel firmness and water-holding capacity and caused a reduction in the extent of gel swelling.
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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
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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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