Abstract
Biosurfactants (BSs) attract increasing attention as sustainable alternatives to petroleum-derived surfactants. This necessitates structural insight into how BSs interact with proteins encountered by current chemical surfactants. Thus, small-angle x-ray scattering (SAXS) has been used for studying the structures of complexes made of the proteins α-Lactalbumin (αLA) and myoglobin (Mb) with the biosurfactant rhamnolipid (RL). For comparison, complexes between αLA and the chemical surfactant sodium dodecyl sulfate (SDS) were also investigated. The SAXS data for pure RL micelles can be described by prolate core-shell structures with a core radius of 7.7 Å and a shell thickness of 12 Å, giving an aggregation number of 11. The small core radius is attributed to RL's complex hydrophobic tail. Data for the αLA-RL complex agree with a 12-molecule micelle with a single protein molecule in the shell. For Mb-RL, the analysis gives complexes of two connected micelles, each containing 10 RL and one protein in the shells. αLA-RL and Mb-RL form surfactant-saturated complexes above 5.6 and 4.7 mM RL, respectively, leaving the remaining RL in free micelles. The SAXS data for SDS agree with oblate-shaped micelles with a core of 20 Å, core eccentricity 0.7, and shell thickness of 5.45 Å, with an aggregation number of 74. The αLA-SDS complexes contain a prolate micelle with a core radius of 11-14 Å and a shell of 8-12 Å with up to 3 αLA per particle and up to 43 SDS per αLA, both considerably larger than for RL. Unlike the RL-protein complexes, the number of surfactant molecules in αLA-SDS complexes increases with surfactant concentration, and saturate at higher surfactant concentrations than αLA-RL complexes. The results highlight how RL and SDS follow similar overall rules of self-assembly and interactions with proteins, but that differences in the strength of protein-surfactant interactions affect the formed structures.