Adsorption properties of soluble surface active stilbazium dyes at the air-water interface

Author(s):  
K. Lunkenheimer ◽  
A. Laschewsky
Langmuir ◽  
2000 ◽  
Vol 16 (17) ◽  
pp. 6982-6986 ◽  
Author(s):  
K. Lunkenheimer ◽  
A. Piasecki ◽  
B. Burczyk ◽  
R. Hirte

1989 ◽  
Vol 56 (3) ◽  
pp. 487-494 ◽  
Author(s):  
Michael Wilson ◽  
Daniel M. Mulvihill ◽  
William J. Donnelly ◽  
Brian P. Gill

Summaryβ-Casein, was enzymically modified by incubation with plasmin to yield γ-caseins and proteose peptones. Whole γ-, γ1-, γ2/γ3-caseins and whole proteose peptone (pp) were isolated from the hydrolysate mixture. The time dependence of surface tension at the air-water interface of solutions of β-casein and its plasmin derived fragments, at concentrations of 10−1 to 10−4% (w/v) protein, pH 7.0, was determined, at 25 °C, using a drop volume apparatus. The ranking of the proteins with respect to rate of reduction of surface tension, during the first rate determining step, at 10-2% (w/v) protein, was γ2/γ3 ≫ pp > whole γ- > γ1- > β-casein. The ranking of the proteins with respect to surface pressures attained after 40 min (π40) was concentration dependent. γ2/γ3-Caseins were found to be very surface active, decreasing surface tension rapidly and giving a high π40. γ1 Casein decreased surface activity somewhat faster than β-casein, but generally reached a lower π40. Whole γ-casein reflected the properties of both γ1 and γ2/γ3-caseins. Proteose peptone was found to decrease surface tension rapidly during the initial rate determining step; it gave a relatively high π40 at a bulk phase concentration of 10−3% (w/v) protein, but, it was the least surface active protein at 10−1 and 10−2% (w/v) protein.


Langmuir ◽  
2017 ◽  
Vol 33 (30) ◽  
pp. 7548-7555 ◽  
Author(s):  
Wei Liu ◽  
Shanghao Li ◽  
Zhuguang Wang ◽  
Elsa C. Y. Yan ◽  
Roger M. Leblanc

Langmuir ◽  
2007 ◽  
Vol 23 (12) ◽  
pp. 6638-6644 ◽  
Author(s):  
Klaus Lunkenheimer ◽  
Gohsuke Sugihara ◽  
Maciej Pietras

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