2010
DOI: 10.1016/j.colsurfb.2009.08.046
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Physico-chemical studies of molecular interactions between non-ionic surfactants and bovine serum albumin

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Cited by 97 publications
(50 citation statements)
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“…There was no significant difference in the EC of polysorbate 20, polysorbate 80 and soy lecithin. This is not in accordance with the study by Ruiz-Peña et al (2010) who reported that polysorbate 80 had higher value of surface excess concentration at surface saturation compared to polysorbate 20. High value of surface excess concentration at surface saturation indicated high effectiveness of adsorption at surface, thereby giving high emulsifying capacity.…”
Section: Emulsifying Capacity Of Emulsifierscontrasting
confidence: 55%
“…There was no significant difference in the EC of polysorbate 20, polysorbate 80 and soy lecithin. This is not in accordance with the study by Ruiz-Peña et al (2010) who reported that polysorbate 80 had higher value of surface excess concentration at surface saturation compared to polysorbate 20. High value of surface excess concentration at surface saturation indicated high effectiveness of adsorption at surface, thereby giving high emulsifying capacity.…”
Section: Emulsifying Capacity Of Emulsifierscontrasting
confidence: 55%
“…SDS and Tween-20 were chosen as points of comparison because their interactions with BSA are well characterized [46][47][48]. SDS and Tween-20 are also structurally similar to POPC and PEGylated lipids (Supporting Information Fig.…”
Section: Comparison Of Popc/dspeg3000 Coating With Anionic and Neutramentioning
confidence: 99%
“…To use them correctly, it is necessary to have an idea of how and in which amounts they interact with proteins. Although surfactant-protein interactions have been widely studied for half a century [1][2][3][4][5], the mechanism of interaction is not well understood. Knowledge of the interactions is not only fundamental in theoretics, but also practical in industrial applications.…”
Section: Introductionmentioning
confidence: 99%