Rheological properties of proteins

Krause, J., Schultz, M., and Dudek, S. 2002. Effect of extraction conditions on composition, surface activity and rheological properties of protein isolates from flaxseed (Linum usitativissimum L). J. Sci. Food Agric. 82, 970-976. 

Sathivel, S., Bechtel, P. J., Babbitt, J. K., Prinyawiwatkul, W., and Patterson, M. 2005. Functional, nutritional, and rheological properties of protein powders from arrow-tooth flounder and their application in mayonnaise. Food Eng. Phys. Prop., 70, 57-63. 

Muhrbeck, P. and Eliasson, A. C. 1991. Rheological properties of protein/starch mixed gels. J. Texture Stud. 22 317-332. 

Ismailova, V.N., "Stmcture Formation and Rheological Properties of Proteins and Surface-Active Polymers of Interfacial Adsorption Layers" in Progress in Surface and Membrane Science 13(1979)... 

Murray, B. S. (2011). Rheological properties of protein films. Current Opinion in Colloid and Interface Science, 16, 27—35. 

The ionic strength dependence of intrinsic viscosity is function of molecular structure and protein folding, ft is well known that the conformational and rheological properties of charged biopolymer solutions are dependent not only upon electrostatic interactions between macromolecules but also upon interactions between biopolymer chains and mobile ions. Due electrostatic interactions the specific viscosity of extremely dilute solutions seems to increase infinitely with decreasing ionic concentration. Variations of the intrinsic viscosity of a charged polyampholite with ionic strength have problems of characterization. 

Rheological measurements were carried out to investigate the rheological properties of emulsions stabilized by different fat-water interfaces and the influence of fat droplets on the formation of the protein networks during a process of gelation. 

T.D. Dimitrova and F. Leal Calderon Rheological Properties of Highly Concentrated Protein-Stabilized Emulsions. Adv. Colloid Interface Sci. 108-109, 49 (2004). 

Bikker, J.F., Anema, S.G., Li, Y., Hill, J.P. (2000). Rheological properties of acid gels prepared front heated milk fortified with whey protein mixtures containing the A, B and C variants of p-lactoglobulin. International Dairy Journal, 10, 723-732. 

Weinbreck, F., Wientjes, R.H.W., Nieuwenhuijse, EL, Robijn, G.W., de Kruif, C.G. (2004b). Rheological properties of whey protein/gum arabic coacervates. Journal of Rheology, 48, 1215-1228... 

Bos, M.A., van Vliet, T. (2001). Interfacial rheological properties of adsorbed protein layers and surfactants. Advances in Colloid and Interface Science, 91, 437-471. 

The term food colloids can be applied to all edible multi-phase systems such as foams, gels, dispersions and emulsions. Therefore, most manufactured foodstuffs can be classified as food colloids, and some natural ones also (notably milk). One of the key features of such systems is that they require the addition of a combination of surface-active molecules and thickeners for control of their texture and shelf-life. To achieve the requirements of consumers and food technologists, various combinations of proteins and polysaccharides are routinely used. The structures formed by these biopolymers in the bulk aqueous phase and at the surface of droplets and bubbles determine the long-term stability and rheological properties of food colloids. These structures are determined by the nature of the various kinds of biopolymer-biopolymer interactions, as well as by the interactions of the biopolymers with other food ingredients such as low-molecular-weight surfactants (emulsifiers). 

Ziegler and Foegeding, 1990. See above. Extensively reviews the rheological properties of various protein gels. Also includes an introduction to gelation theories. 

Huang, X.L., Catignani, G.L., and Swaisgood, H.E. 1999. Modification of the rheological properties of whey protein isolates by limited proteolysis. Nahrung 43, 79-85. 

Complementing these hydrodynamic issues has been an ongoing effort to examine the rheological properties of blood as well as other body fluids. Blood exhibits shear thinning behavior and appears to have a yield stress owing to the formation of macroscopic structures that incorporate protein-aided bridging of red cells. 

Disulfide bonds between proteins have an energy of 49 kcal/mole and are not broken at room temperature except as the result of a chemical reaction. The effects of oxidizing agents on the rheological properties of dough... 

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