Study of the relationship between applied transmembrane pressure and antimicrobial activity of lysozyme
| Autor: | Arnaud Ponche, Ariane de Espindola, Simona M. Miron, Patrick Dutournié |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Biomaterials - proteins
Science Ultrafiltration 02 engineering and technology 010402 general chemistry 01 natural sciences Article law.invention chemistry.chemical_compound Protein structure Chemical engineering law Pressure Filtration chemistry.chemical_classification Multidisciplinary Chemistry Biomolecule Membranes Artificial 021001 nanoscience & nanotechnology 0104 chemical sciences Anti-Bacterial Agents Membrane Enzyme Biophysics Medicine Muramidase Lysozyme 0210 nano-technology Antibacterial activity |
| Zdroj: | Scientific Reports Scientific Reports, Vol 11, Iss 1, Pp 1-8 (2021) |
| ISSN: | 2045-2322 |
| Popis: | During the processing of biomolecules by ultrafiltration, the lysozyme enzyme undergoes conformational changes, which can affect its antibacterial activity. Operational conditions are considered to be one of the main parameters responsible for such changes, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can result in different properties of the protein after filtration, due to their different pore network. The filtration of lysozyme, regardless of the membrane, produces a decrease in the membrane hydraulic permeability (between 10 and 30%) and an increase in its selectivity in terms of observed rejection rate (30%). For the filtrated lysozyme, it appears that the HPLC retention time increases depending on the membrane used. The antibacterial activity of the filtrated samples is lower than the native protein and decreases with the increase of the applied pressure reaching 55–60% loss for 12 bar which has not been reported in the literature before. The observed results by SEC-HPLC and bacteriological tests, suggest that the conformation of the filtrated molecules are indeed modified. These results highlight the relationship between protein conformation or activity and the imposed shear stress. |
| Databáze: | OpenAIRE |
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