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  4. Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation
 
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Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation

Citation Link: https://doi.org/10.15480/882.3193
Publikationstyp
Journal Article
Date Issued
2020-01-31
Sprache
English
Author(s)
Uttinger, Maximilian J.  
Heyn, Timon R.  
Jandt, Uwe  
Wawra, Simon E.  
Winzer, Bettina  
Keppler, Julia K.  
Peukert, Wolfgang  
Institut
Bioprozess- und Biosystemtechnik V-1  
TORE-DOI
10.15480/882.3193
TORE-URI
http://hdl.handle.net/11420/7687
Journal
European biophysics journal  
Volume
49
Issue
8
Start Page
745
End Page
760
Citation
European Biophysics Journal 49 (8): 745-760 (2020)
Publisher DOI
10.1007/s00249-020-01421-4
Scopus ID
2-s2.0-85078800715
Publisher
Springer
The whey protein beta-lactoglobulin is the building block of amyloid fibrils which exhibit a great potential in various applications. These include stabilization of gels or emulsions. During biotechnological processing, high shear forces lead to fragmentation of fibrils and therefore to smaller fibril lengths. To provide insight into such processes, pure straight amyloid fibril dispersions (prepared at pH 2) were produced and sheared using the rotor stator setup of an Ultra Turrax. In the first part of this work, the sedimentation properties of fragmented amyloid fibrils sheared at different stress levels were analyzed with mulitwavelength analytical ultracentrifugation (AUC). Sedimentation data analysis was carried out with the boundary condition that fragmented fibrils were of cylindrical shape, for which frictional properties are known. These results were compared with complementary atomic force microscopy (AFM) measurements. We demonstrate how the sedimentation coefficient distribution from AUC experiments is influenced by the underlying length and diameter distribution of amyloid fibrils. In the second part of this work, we show how to correlate the fibril size reduction kinetics with the applied rotor revolution and the resulting energy density, respectively, using modal values of the sedimentation coefficients obtained from AUC. Remarkably, the determined scaling laws for the size reduction are in agreement with the results for other material systems, such as emulsification processes or the size reduction of graphene oxide sheets.
Subjects
Amyloid fibrils
Analytical ultracentrifugation
Atomic force microscopy
Beta-lactoglobulin
Sedimentation analysis
DDC Class
570: Biowissenschaften, Biologie
600: Technik
Funding(s)
EnzymAgglo - Multiskalige modellgestützte Untersuchungen der Formation von katalytisch aktiven Clustern und Agglomeraten großer Multienzymkomplexe  
Teilprojekt von SPP 1934: Multiskalige modellgestützte Untersuchungen funktionaler Enzym- und Proteinagglomerate für biotechnologische Anwendung - Teil 2: Von der Struktur zur Funktion  
More Funding Information
Acknowledgements Open Access funding provided by Projekt DEAL.
Publication version
publishedVersion
Lizenz
https://creativecommons.org/licenses/by/4.0/
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