Surface and emulsifying properties of caseins

1989 ◽  
Vol 56 (3) ◽  
pp. 471-477 ◽  
Author(s):  
Eric Dickinson

SummaryThe properties of adsorbed films of αs1-, β- and κ-casein and sodium caseinate are compared at the planar oil–water interface, at the surface of emulsion droplets, and at the surface of polystyrene latex particles. Attention is directed towards understanding (i) the relationship between the molecular characteristics of the caseins and their surface activities and surface viscosities at the oil–water interface, (ii) the nature of competitive adsorption between the caseins (particularly αs1- and β-), and (iii) the effect of Na and Ca ion concentrations on electrophoretic mobilities and flocculation behaviour.

Langmuir ◽  
2009 ◽  
Vol 25 (17) ◽  
pp. 10026-10037 ◽  
Author(s):  
Laureline S. Jourdain ◽  
Christophe Schmitt ◽  
Martin E. Leser ◽  
Brent S. Murray ◽  
Eric Dickinson

1985 ◽  
Vol 14 (1) ◽  
pp. 135-141 ◽  
Author(s):  
Eric Dickinson ◽  
David J. Pogson ◽  
Elizabeth W. Robson ◽  
George Stainsby

2012 ◽  
Vol 132 (4) ◽  
pp. 1822-1829 ◽  
Author(s):  
Liya Liu ◽  
Qiangzhong Zhao ◽  
Tongxun Liu ◽  
Jing Kong ◽  
Zhao Long ◽  
...  

Langmuir ◽  
2014 ◽  
Vol 30 (41) ◽  
pp. 12164-12170 ◽  
Author(s):  
KyuHan Kim ◽  
Kyuheong Park ◽  
Gahee Kim ◽  
Hyunjung Kim ◽  
Myung Chul Choi ◽  
...  

1952 ◽  
Vol 5 (1) ◽  
pp. 189
Author(s):  
CWN Cumper ◽  
AE Alexander

The results presented in Part II of this series on the adsorption of the proteins, β-globulin, pepsin, and insulin at a white oil, 5 per cent, oleyl alcohol-water interface have been extended to the petrol ether-water and air-water interfaces by studying the surface rigidity of the films formed. The previous picture of the process of adsorption has been generally confirmed but there are certain differences between the oil-water and air-water interfaces which are discussed.


With the use of a surface rheometer especially designed for the purpose, stress-relaxation phenomena have been studied in unimolecular films of bovine serum album in, pepsin, poly-a, L-lysine (d.p. 15) and sodium arabinate at the hydrocarbon/water interface. The behaviour of the films has been analyzed in terms of the constituent rheological elements and the relaxation spectra have been obtained. From the dependence of the relaxation spectra on temperature, the activation energies for the relaxation of the films have been found. The relationship of these energies to the hydrogen bond energy (which, it was shown in part I, is largely responsible for the observed visco-elasticity) has been discussed.


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