scholarly journals STUDY OF THE SOLUBILIZING CAPACITY OF POLYMER-COLLOID COMPLEXES FORMED WITH SODIUM ALGINATE AND CHLORIDE HEXADECYLPYRIDINIUM

2021 ◽  
Vol 26 (2(78)) ◽  
pp. 40-47
Author(s):  
A. F. Tymchuk ◽  
A. O. Grossu ◽  
A. V. Babenko

It was examined the behavior of systems which contain surfactants and biopolymers is considered by the example of cationic surfactants and sodium alginate. The rheological and surface-active properties of the systems have been experimentally investigated. It was found that the presence of oppositely charged surfactants in the solution significantly affects the properties of sodium alginate, due to the fact that associates or polymer-colloidal complexes are formed in the solution. Their formation significantly affects the solubilizing ability in relation to non-polar liquids. Hydrodynamic parameters of macromolecules of sodium alginate in comparison with macromolecules of chitosan correspond to the conformation of the loose ball. The state of the SN is determined by the pH of the medium and temperature. The increase in temperature leads to a violation of the structure of the chain, its destruction and a subsequent decrease in viscosity. At a temperature of 293K, the macromolecule is in a more ordered state. In the alkaline environment there is a change in the conformation of the macromolecule. As a result of this change, the viscosity naturally increases. This is explained by the fact that in an alkaline environment, the macromolecule acquires an excess negative charge, there is a repulsion of the carboxyl groups of the same name in the chain links. The macromolecule acquires an expanded configuration. The viscosity increases. In acidic environment, sodium alginate has almost zero charge as a result of protonation of carboxyl groups. The molecule acquires the conformation of a loose ball with the lowest value of viscosity. The isoelectric state of the alginate macromolecule is observed in the pH range of 5.5 to 6.0. The described state of the macromolecule in solution is confirmed by our calculations. The interaction of surface-active cations with carboxyl groups of SN leads first to the formation of associates, then to polymer-colloidal complexes. The association as a result of electrostatic interaction of active groups is enhanced by the hydrophobic interaction of hydrocarbon fragments of surfactant molecules with each other and with the alginate matrix. The association ends with the formation of a polymer-colloidal complex.

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

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

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

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.


Sign in / Sign up

Export Citation Format

Share Document