Synthesis of EDTA-monoalkyl ester chelates and evaluation of the surface active properties

1980 ◽  
Vol 57 (12) ◽  
pp. 430-434 ◽  
Author(s):  
Toshio Takeshita ◽  
Izumi Wakebe ◽  
Shigeru Maeda
Keyword(s):  
Surface Active Properties ◽  
Monoalkyl Ester ◽  
Surface Active

scholarly journals Research of surface-active properties and sizes of pectin molecules after post-alcohol grain distillery dreg

2021 ◽  
Vol 640 (5) ◽  
pp. 052014
Author(s):  
A S Kaishev ◽  
N S Kaisheva ◽  
H N Gyulbyakova ◽  
E A Maslovskaya ◽  
V A Karpenko
Keyword(s):  
Surface Active Properties ◽  
Surface Active

Surface active properties of viscosin: a peptidolipid antibiotic

1990 ◽  
Vol 32 (5) ◽  
Author(s):  
ThomasR. Neu ◽  
Thomas H�rtner ◽  
Karl Poralla
Keyword(s):  
Surface Active Properties ◽  
Surface Active

Antimicrobial and surface-active properties of cationic surfactants based on chloroalkanes and alkylbenzenes

1984 ◽  
Vol 18 (11) ◽  
pp. 784-787 ◽  
Author(s):  
M. A. Chernyavskaya ◽  
V. V. Stefanovich ◽  
I. A. Sergeeva ◽  
A. S. Belova
Keyword(s):  
Cationic Surfactants ◽  
Surface Active Properties ◽  
Surface Active

Surface active properties at the air–water interface of β-casein and its fragments derived by plasmin proteolysis

1989 ◽  
Vol 56 (3) ◽  
pp. 487-494 ◽  
Author(s):  
Michael Wilson ◽  
Daniel M. Mulvihill ◽  
William J. Donnelly ◽  
Brian P. Gill
Keyword(s):  
Surface Tension ◽  
Water Interface ◽  
Active Protein ◽  
Drop Volume ◽  
V Protein ◽  
Proteose Peptone ◽  
Rate Determining Step ◽  
Surface Active Properties ◽  
Air Water Interface ◽  
Surface Active

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.

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