2008
DOI: 10.1016/j.colsurfa.2007.10.027
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Effect of surface potential of reverse micelle on enzyme–substrate complex formation

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Cited by 10 publications
(4 citation statements)
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“…Accordingly, Triton X-100 increased enzyme partitioning compared with Tween-80, and SDS, which is an anionic surfactant, produced the smallest effect on enzyme partitioning. It has previously been suggested that ionic surfactant molecules bound to proteins might interrupt the tertiary structures of those proteins, and the interaction between ionic surfactants and proteins has been verified to be mediated via a combination of electrostatic and hydrophobic forces [ 24 , 25 ]. Therefore, the surfactant head group plays a determining role in protein-surfactant interactions that preferentially begin with strong ionic bond formation between the surfactant polar groups [ 26 ].…”
Section: Resultsmentioning
confidence: 99%
“…Accordingly, Triton X-100 increased enzyme partitioning compared with Tween-80, and SDS, which is an anionic surfactant, produced the smallest effect on enzyme partitioning. It has previously been suggested that ionic surfactant molecules bound to proteins might interrupt the tertiary structures of those proteins, and the interaction between ionic surfactants and proteins has been verified to be mediated via a combination of electrostatic and hydrophobic forces [ 24 , 25 ]. Therefore, the surfactant head group plays a determining role in protein-surfactant interactions that preferentially begin with strong ionic bond formation between the surfactant polar groups [ 26 ].…”
Section: Resultsmentioning
confidence: 99%
“…It is important to note that the effect of surfactants on the enzyme partitioning depends on selective chemical interactions between the enzyme molecules and surfactant. This effect is further divided into two factors which are: (i) structure of the enzyme and (ii) the chemical properties of the surfactant [30]. The results in Table 2 indicate that the selectivity and purification factors of the lipase in a non-ionic surfactant/xylitol system are significantly higher ( p < 0.05) compared to an ionic ATPS.…”
Section: Resultsmentioning
confidence: 99%
“…Ermakova et al [33] studied the effect of surface potential of reversed micelle on enzyme-substrate complex (encounter complex, EC) formation by Brownian dynamics simulation. The research pointed out that the negative potential of micelle increases the probability of EC formation and the positive potential decreases it.…”
Section: Electrostatic Interactionsmentioning
confidence: 99%