The study of protein and surfactant interactions is of great significance in a number of applications, such as the cosmetic, food or pharmaceutical industries and many others. However, they require further study due to their compositional complexity and the limitations of current analytical approaches. In this thesis, the cationic surfactant septonex in combination with two differently charged proteins lysozyme and bovine serum albumin under different physiological conditions (temperature, surfactant concentration, environment and others) was selected to study the interactions. Characterization of protein-surfactant interactions is a very important but challenging task, therefore it is essential to use appropriate approaches to explore the nature of these interactions. In order to unify the information to provide rational models, calorimetric methods (DSC, ITC) and dynamic light scattering were used. Isothermal titration calorimetry monitors the evidence for the formation of the system of the mentioned substances and information on aggregation behavior, differential scanning calorimetry characterizes the thermal stability of proteins and dynamic light scattering made it possible to monitor changes in particle size. Both proteins have been proven to interact with positive septonex, even if the lysozyme molecule is also positively charged. However, significant differences were found between the two proteins. From the obtained results it is evident that the identical charge of the protein with the surfactant has an effect on the intensity of the measurement, although all measured interactions showed an endothermic character.
| Identifer | oai:union.ndltd.org:nusl.cz/oai:invenio.nusl.cz:449410 |
| Date | January 2021 |
| Creators | Bohunská, Miroslava |
| Contributors | Pekař, Miloslav, Krouská, Jitka |
| Publisher | Vysoké učení technické v Brně. Fakulta chemická |
| Source Sets | Czech ETDs |
| Language | Czech |
| Detected Language | English |
| Type | info:eu-repo/semantics/masterThesis |
| Rights | info:eu-repo/semantics/restrictedAccess |
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