Lactoglobulin adsorption

Cornec, M., Narsimhan, G. (2000). Adsorption and exchange of (3-lactoglobulin onto spread monoglyceride monolayers at the air-water interface. Fangmuir, 16, 1216-1225. 

Cornec, M., Mackie, A.R., Wilde, P.J., Clark, D.C. (1996). Competitive adsorption of p-lactoglobulin and p-casein with Span 80 at the oil-water interface and the effect on emulsion behaviour. Colloids and Surfaces A Physicochemical and Engineering Aspects, 114, 237-244. 

Horne, D.S., Atkinson, P.J., Dickinson, E., Pinfield, V.J., Richardson, R.M. (1998). Neutron reflectivity study of competitive adsorption of p-lactoglobulin and non-ionic surfactant at the air-water interface. International Dairy Journal, 8, 73-77. 

Mackie, A.R., Husband, F.A., Holt, C., Wilde, P.J. (1999a). Adsorption of (3-lactoglobulin variants A and B to the air-water interface. International Journal of Food Science and Technology, 34, 509-516. 

Krisdhasima, V., Vinaraphong, R, and McGuire, J. 1993. Adsorption kinetics and elutability of a-lactalbumin, p-casein, p-lactoglobulin and bovine serum albumin at hydrophobic and hydrophilic interfaces. J. Colloid Interface Sci. 161 325-334. 

The adsorption of albumin from aqueous solution onto copper and nickel films and the adsorption of B-lactoglobulin, gum arabic, and alginic acid onto germanium were studied. Thin metallic films (3-4 nm) were deposited onto germanium internal reflection elements by physical vapor deposition. Transmission electron microscopy studies indicated that the deposits were full density. Substrate temperature strongly Influenced the surface structure of the metal deposits. Protein and/or polysaccharide were adsorbed onto the solid substrates from flowing... 

Figure 9. Kinetic plot for 0.01% (w v) B-lactoglobulin and 1.0% (w v) alginic acid adsorption on and desorption from germanium ATR crystal as a function of time of flow. Key D1548 cm 1 band of 13-lactoglobulin 1034 cm 1 band of alginic acid. (All data not shown for clarity.)...

Benhamou and Guastalla (1960) were the first to question the assumption of irreversibility with an analysis of the adsorption of insulin, /3-lactoglobulin, and ribonuclease. They investigated whether the Gibbs adsorption equation was obeyed. This basic equation, applicable to reversible adsorption, is firmly based on thermodynamics and has been amply verified experimentally. It can be written in the simple form... 

The supercooling is also observed with protein (BSA, casein, lactoglobulin) in addition to the aqneous phase-Cjg system, bnt the freezing point of hexadecane increases to 18.2°C. This indicates that the crystallization of the hexadecane is affected by the presence of surface-active molecules. The supercooling will have extensive dependence on various interfaces, such as emulsions, oil recovery, and immunological systems. The adsorption of proteins from aqueous solutions on snrfaces has been studied by neutron reflection. ... 

The surfactant /1-lactoglobulin is a small protein molecule that does not strongly unfold upon adsorption at the O-W interface (Section 10.3.2). Consequently, stability against aggregation will primarily be due to electrostatic repulsion. The dilution with water will lower the ionic strength by about a factor of 2. It can be seen in Figure 13.4 that this will cause a considerable increase in W, e.g., by a factor of 50. Moreover, the larger W value will cause an increase in the value of D, which will also increase the gel time. 

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