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Research Article
patrick dutournie
University of Upper Alsace
Corresponding Author
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During the processing of biomolecules by ultrafiltration, the lysozyme enzyme suffers conformational changes, which can affect its antibacterial activity. Operational conditions are considered ones of the principal responsible for the modifications, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can produce different properties on 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 10–30%) 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 is not reported in the literature. 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.
Keywords
lysozyme, antibacterial activity, ultrafiltration, HPLC, protein conformation
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No competing interests reported.
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On 12 Apr, 2021
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This preprint is under consideration at Scientific Reports. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
patrick dutournie
University of Upper Alsace
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 23 Mar, 2021
No community comments so far
Editorial decision: Major revision
On 12 Apr, 2021
Reviews received
Received 06 Apr, 2021
Reviewers agreed
On 04 Apr, 2021
Reviewers agreed
On 25 Mar, 2021
Reviewers invited
Invitations sent on 23 Mar, 2021
Editor assigned
On 23 Mar, 2021
Editor invited
On 22 Mar, 2021
Submission checks complete
On 22 Mar, 2021
First submitted
On 17 Mar, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
During the processing of biomolecules by ultrafiltration, the lysozyme enzyme suffers conformational changes, which can affect its antibacterial activity. Operational conditions are considered ones of the principal responsible for the modifications, especially when using the same membrane and molecule. The present study demonstrates that, the same cut-off membrane (commercial data) can produce different properties on 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 10–30%) 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 is not reported in the literature. 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.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
No competing interests reported.
This is a list of supplementary files associated with this preprint. Click to download.
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