Studies
of protein-surfactant interactions go back about a century, being inspired by
broad practical implications. There is extensive literature on this topic.
However, most of the publications concentrate on the effect of surfactants on
proteins, such as the unfolding and refolding of the protein coil, and the
application of surfactants in isolation and purification of proteins,
especially those incorporated into biological membranes.
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| Proteins as Surfactant Enhancers |
For water-soluble
proteins, interactions with surfactants were broadly split up into two regions:
below and above the surfactant’s critical micelle concentration (CMC). With
anionic surfactants (such as sodium lauryl sulfate) the binding to a protein
(such as lysozyme) starts before the surfactant’s CMC is achieved, leading to a
plateau in the Gibbs isotherm at 15 to 20 surfactant molecules bound to each
protein globule. After the CMC has been surpassed, further steep growth of
binding was found. Read More>>>>>>>>
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