Protein emulsifying property

Britten, M., Giroux, H.J., Jean, Y, and Rodrigue, N. 1994. Composite blends from heat-denatured and undenatured whey protein Emulsifying properties. International Dairy Journal 4 25-36. 

Protein Emulsifying property Whipping property Gelation property Film formation Environmental stability... 

Deamidation of soy and other seed meal proteins by hydrolysis of the amide bond, and minimization of the hydrolysis of peptide bonds, improves functional properties of these products. For example, treatment of soy protein with dilute (0.05 A/) HCl, with or without a cation-exchange resin (Dowex 50) as a catalyst (133), with anions such as bicarbonate, phosphate, or chloride at pH 8.0 (134), or with peptide glutaminase at pH 7.0 (135), improved solubiHty, whipabiHty, water binding, and emulsifying properties. 

Akhtar, M., Dickinson, E. (2003). Emulsifying properties of whey protein-dextran conjugates at low pH and different salt concentrations. Colloids and Surfaces B Biointerfaces, 31, 125-132. 

Dickinson, E., Semenova, M.G. (1992). Emulsifying properties of covalent protein-dex-tran hybrids. Colloids and Surfaces, 64, 299-310. 

Leman, I, Kinsella, J.E. (1989). Surface activity, film formation, and emulsifying properties of milk proteins. Critical Reviews in Food Science and Nutrition, 28, 115-138. 

Mitchell, J.R. (1986). Foaming and emulsifying properties of proteins. In Hudson, B.J.F. (Ed.). Developments in Food Proteins 4, London Elsevier Applied Science, pp. 291-338. 

In proposing these divisions, one must acknowledge that hybrid properties are certainly possible. Thus, an emulsifying property of a protein might be used as a sense enhancing one— to prepare a smooth food product—or a manipulative one—to provide even subdivision for uniform administration. 

The methodological factors having a special influence on these tests of emulsifying properties are subdivision methods for the colloidal system, ratio of components (water protein oil), and the nature of the fat used. The second one is the most neglected of these influences and is usually chosen by the researcher at will. 

Emulsifying Properties of Selected Vegetable Protein Sources... 

Figure 10. Solubility and emulsifying properties of cottonseed proteins at various...

Alkali treatment is used to solubilize and isolate proteins, to improve foaming and emulsifying properties, and to obtain protein solutions suitable for spinning fibers (17) ... 

Emulsification is a stabilizing effect of proteins a lowering of the interfacial tension between immiscible components that allow the formation of a protective layer around oil droplets. The inherent properties of proteins or their molecular conformation, denaturation, aggregation, pH solubility, and susceptibility to divalent cations affect their performance in model and commercial emulsion systems. Emulsion capacity profiles of proteins closely resemble protein solubility curves and thus the factors that influence solubility properties (protein composition and structure, methods and conditions of extraction, processing, and storage) or treatments used to modify protein character also influence emulsifying properties. 

Arteaga, G.E. and Nakai, S. 1993. Predicting protein functionality with artificial neural networks Foaming and emulsifying properties. J. FoodSci. 58 1152-1156. 

Pearce, K.N. and Kinsella, J.E. 1978. Emulsifying properties of proteins Evaluation of a turbidimetric technique. J. Agric. Food Chem. 26 7lb-723. 

Arteaga, G.E. 1994. Assessment of protein surface hydrophobicity by spectroscopic methods and its relation to emulsifying properties of proteins. Ph.D. Thesis, University of British Columbia, Vancouver, B.C., Canada. 

A.N. Gurov, M.A. Mukhin, N.A. Larichev, N.V. Lozinskaya and V.B. Tolstoguzov, Emulsifying properties of proteins and polysaccharides, I, Methods of determination of emulsifying capacity and emulsion stability, Colloids Surfaces 6 (1983) 35-42. 

Gum arabic is covalently bonded to approximately 2% protein that is believed to confer exceptional emulsifying properties (Dickinson and Euston, 1991a Randall et al., 1988). Anderson (1988) located varying proportions of amino acids at the periphery and in the interior of the complex. 

Since the emulsifying properties depend on the balance between hydro-phobicity and hydrophilicity at the protein surface, a very high yield of phosphorylation may disrupt this balance. The higher improvement of emulsifying properties of K-casein was due to its original high hydro-phobicity, which diminished after phosphorylation. 

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