Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Impact of surfactant additions on dynamic properties of β-casein adsorption layers. / Latnikova, A. V.; Lin, S. Y.; Loglio, G.; Miller, R.; Noskov, B. A.
в: Journal of Physical Chemistry C, Том 112, № 15, 17.04.2008, стр. 6126-6131.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Impact of surfactant additions on dynamic properties of β-casein adsorption layers
AU - Latnikova, A. V.
AU - Lin, S. Y.
AU - Loglio, G.
AU - Miller, R.
AU - Noskov, B. A.
PY - 2008/4/17
Y1 - 2008/4/17
N2 - The dynamic surface elasticity of solutions of β-casein/surfactant mixtures was measured as a function of surface age and surfactant concentration. Small additions of ionic surfactants changed strongly the kinetic dependence of the dynamic surface elasticity of protein solutions. The shape of the kinetic curve depended on the charge of the surfactant ion. The results can be explained by strong electrostatic interactions between charged amino acid residues in the protein and surfactant ions, and different distributions of positive and negative charges along the protein chain. It is shown that small additions of ionic surfactants can probe the mechanism of protein adsorption. The obtained results confirm the consecutive transitions of the relatively hydrophilic and hydrophobic parts of a β-casein molecule into the subphase as loops and tails. Unlike the case of β-casein/ionic surfactant solutions, the effect of small additions of a nonionic surfactant with high surface activity can be described as a gradual displacement of /5-casein from the adsorption layer.
AB - The dynamic surface elasticity of solutions of β-casein/surfactant mixtures was measured as a function of surface age and surfactant concentration. Small additions of ionic surfactants changed strongly the kinetic dependence of the dynamic surface elasticity of protein solutions. The shape of the kinetic curve depended on the charge of the surfactant ion. The results can be explained by strong electrostatic interactions between charged amino acid residues in the protein and surfactant ions, and different distributions of positive and negative charges along the protein chain. It is shown that small additions of ionic surfactants can probe the mechanism of protein adsorption. The obtained results confirm the consecutive transitions of the relatively hydrophilic and hydrophobic parts of a β-casein molecule into the subphase as loops and tails. Unlike the case of β-casein/ionic surfactant solutions, the effect of small additions of a nonionic surfactant with high surface activity can be described as a gradual displacement of /5-casein from the adsorption layer.
UR - http://www.scopus.com/inward/record.url?scp=47149095258&partnerID=8YFLogxK
U2 - 10.1021/jp712107n
DO - 10.1021/jp712107n
M3 - Article
AN - SCOPUS:47149095258
VL - 112
SP - 6126
EP - 6131
JO - Journal of Physical Chemistry C
JF - Journal of Physical Chemistry C
SN - 1932-7447
IS - 15
ER -
ID: 13746523