Relevant bibliographies by topics / Beta-lactoglobulin fibrils

Academic literature on the topic 'Beta-lactoglobulin fibrils'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Beta-lactoglobulin fibrils"

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Uttinger, Maximilian J., Timon R. Heyn, Uwe Jandt, Simon E. Wawra, Bettina Winzer, Julia K. Keppler, and Wolfgang Peukert. "Measurement of length distribution of beta-lactoglobulin fibrils by multiwavelength analytical ultracentrifugation." European Biophysics Journal 49, no. 8 (January 31, 2020): 745–60. http://dx.doi.org/10.1007/s00249-020-01421-4.

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AbstractThe 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.
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Kayser, Jil J., Philipp Arnold, Anja Steffen-Heins, Karin Schwarz, and Julia K. Keppler. "Functional ethanol-induced fibrils: Influence of solvents and temperature on amyloid-like aggregation of beta-lactoglobulin." Journal of Food Engineering 270 (April 2020): 109764. http://dx.doi.org/10.1016/j.jfoodeng.2019.109764.

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3

Al-Shabib, Nasser Abdulatif, Javed Masood Khan, Ajamaluddin Malik, Abdulrahman M. Alsenaidy, Mohammad A. Alsenaidy, Fohad Mabood Husain, Monis Bilal Shamsi, Syed Hidayathulla, and Rizwan Hasan Khan. "Negatively charged food additive dye “Allura Red” rapidly induces SDS-soluble amyloid fibril in beta-lactoglobulin protein." International Journal of Biological Macromolecules 107 (February 2018): 1706–16. http://dx.doi.org/10.1016/j.ijbiomac.2017.10.032.

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4

Heyn, Timon R., Vasil M. Garamus, Hendrikje R. Neumann, Maximilian J. Uttinger, Tobias Guckeisen, Monique Heuer, Christine Selhuber-Unkel, Wolfgang Peukert, and Julia K. Keppler. "Influence of the polydispersity of pH 2 and pH 3.5 beta-lactoglobulin amyloid fibril solutions on analytical methods." European Polymer Journal 120 (November 2019): 109211. http://dx.doi.org/10.1016/j.eurpolymj.2019.08.038.

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Book chapters on the topic "Beta-lactoglobulin fibrils"

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Loveday, Simon, M. Anandha Rao, and Harjinder Singh. "Beta-Lactoglobulin Fibril Dispersions: Structural and Rheological Characteristics." In Global Food Security and Wellness, 295–300. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6496-3_15.

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