Despite a very large number of bacterial exopolysaccharides have been reported, detailed knowledge on their molecular structures and associative interactions with proteins is lacking. Small-angle X-ray scattering, dynamic light scattering and analytical ultracentrifugation (AUC) were used to characterize the interactions of six lactic acid bacterial heteroexopolysaccharides (HePS-1-HePS-6) with β-lactoglobulin (BLG). Compared to free HePSs, a large increase in the X-ray radius of gyration RG, maximum length L and hydrodynamic diameter dH of HePS-1-HePS-4 mixed with BLG revealed strong aggregation, the extent of which depended on the compact conformation and degree of branching of these HePSs. No significant effects were observed with HePS-5 and HePS-6. Turbidity and AUC analyses showed that both soluble and insoluble BLG-HePS complexes were formed. The findings provide new insights into the role of molecular structures in associative interactions between HePSs and BLG which has relevance for various industrial applications.
|Journal||International Journal of Biological Macromolecules|
|Number of pages||9|
|Publication status||Published - 2018|
- Analytical ultracentrifugation
- Dynamic light scattering
- Small-angle X-ray scattering
Khan, S., Birch, J., Van Calsteren, M-R., Ipsen, R., Peters, G. H. J., Svensson, B., Harris, P., & Almdal, K. (2018). Interaction between structurally different heteroexopolysaccharides and β-lactoglobulin studied by solution scattering and analytical ultracentrifugation. International Journal of Biological Macromolecules, 111, 746-754. https://doi.org/10.1016/j.ijbiomac.2018.01.050