On the validity of the optimum micelle size approach in the study of micellar solutions

1987 ◽  
Vol 119 (1) ◽  
pp. 211-227 ◽  
Author(s):  
I.V Rao ◽  
E Ruckenstein
Keyword(s):  
Micellar Solutions ◽  
Micelle Size

Effect of cetyltrimethylammonium bromide on the electrochemiluminiscence and electrooxidation of luminol

1983 ◽  
Vol 48 (2) ◽  
pp. 477-483 ◽  
Author(s):  
Jan Lasovský ◽  
František Grambal
Keyword(s):  
Cetyltrimethylammonium Bromide ◽  
Linear Sweep Voltammetry ◽  
Critical Micellar Concentration ◽  
Peak Height ◽  
Anodic Peak ◽  
Alkaline Solutions ◽  
Platinum Electrodes ◽  
Micellar Solutions ◽  
Linear Sweep ◽  
Low Concentrations

The electrooxidation of luminol in alkaline solutions in the presence of cetyltrimethylammonium bromide (I) was studied by linear sweep voltammetry on fixed and vibrating platinum electrodes. The presence of I in low concentrations (below the critical micellar concentration) brings about aggregation of the luminol, which is manifested by an increase in the anodic peak height and its shift towards lower potentials. In micellar solutions the peak height decreases owing to the slower diffusion of the bulkier micelles, the shift to lower potentials being preserved. The light-voltage curves correspond with the voltammetric curves, exhibiting identical shifts of the peak potentials in dependence on the concentration of the surfactant.

Hydration of Aliphatic Aldehydes in Micellar Solutions

1988 ◽  
Vol 25-26 ◽  
pp. 335-338
Author(s):  
Wilhelm Knoche ◽  
Victoria R. Hanke ◽  
Edward Dutkiewicz
Keyword(s):  
Micellar Solutions ◽  
Aliphatic Aldehydes

Contribution of casein micelle size and proteolysis on protein distribution and sediment formation in UHT milk during storage

2021 ◽  
Vol 117 ◽  
pp. 104980
Author(s):  
Marije Akkerman ◽  
Lene Buhelt Johansen ◽  
Valentin Rauh ◽  
Nina Aagaard Poulsen ◽  
Lotte Bach Larsen
Keyword(s):  
Casein Micelle ◽  
Protein Distribution ◽  
Uht Milk ◽  
Micelle Size ◽  
Sediment Formation

Hydrophobic interactions in human casein micelle formation: β-casein aggregation

1989 ◽  
Vol 56 (3) ◽  
pp. 427-433 ◽  
Author(s):  
Charles W. Slattery ◽  
Satish M. Sood ◽  
Pat Chang
Keyword(s):  
Light Scattering ◽  
Conformational Transition ◽  
Hydrophobic Interactions ◽  
Micelle Formation ◽  
Tryptophan Fluorescence ◽  
Phosphate Esters ◽  
Casein Micelle ◽  
Protein Association ◽  
P Protein ◽  
Micelle Size

SummaryThe association of non-phosphorylated (0-P) and fully phosphorylated (5-P) human β-caseins was studied by fluorescence spectroscopy and laser light scattering. The tryptophan fluorescence intensity (FI) level increased between 20 and 35 °C, indicating a change in the environment of that residue. A similar transition occurred when ANS was used as a probe. Transition temperatures were slightly lower in 10 mM-CaCl2 but were not affected by an equivalent increase in ionic strength caused by NaCl. The magnitude of the FI change was less for the 5-P than the 0-P protein but was increased for both by CaCl2 addition. These FI data were characteristic of a conformational change and this was supported by fluorescence polarization which indicated that with CaCl2, tryptophan and ANS mobility increased at the transition temperature even though the extent of protein association also increased. Light scattering suggested that protein association proeeeded with the primary formation of submicellar aggregates containing 20–30 monomers which then associated further to form particles of minimum micelle size (12–15 submicelles), and eventually larger. The temperature of precipitation of the 5-P form in the presence of CaCl2 was lower than the conformational transition and suggested that both hydrophobic interactions and Ca bridges between phosphate esters on adjacent molecules are important in micelle formation.

Sign in / Sign up

Export Citation Format

Share Document