Zobrazeno 1 - 10
of 241
pro vyhledávání: '"R Heyn"'
Publikováno v:
Food Hydrocolloids 139 (2023)
Food Hydrocolloids, 139
Food Hydrocolloids, 139
In this study beta-lactoglobulin solutions were processed with glass beads in an orbital shaker at high temperatures and low pH value to identify the effect of mechanical stressing and surfaces on amyloid aggregation kinetics. The information will pr
Autor:
Wei Xiang, Alice Drobny, Friederike Zunke, Karin Schwarz, Timon R. Heyn, Bisher Eymsh, Julia K. Keppler, Philipp Arnold, Ralph Lucius
Publikováno v:
Biomacromolecules 21 (2020) 12
Biomacromolecules, 21(12), 4673-4684
Biomacromolecules, 21(12), 4673-4684
Alpha-synuclein (aSyn) is a cytosolic, aggregation-prone protein that is associated with neurodegenerative disorders like Parkinson’s disease. Interestingly, the protein can appear in different conformations, including monomeric and oligomeric form
Autor:
M. J. Uttinger, C. S. Hundschell, V. Lautenbach, S. Pusara, S. Bäther, T. R. Heyn, J. K. Keppler, W. Wenzel, J. Walter, M. Kozlowska, A. M. Wagemans, W. Peukert
Publikováno v:
Soft Matter, 18, 6739-6756
Soft Matter 18 (2022)
Soft Matter 18 (2022)
Protein-protein interactions are essential for the understanding of biological processes. Specific protein aggregation is an important aspect for many biological systems. In particular, electrostatic interactions play the key role for protein-protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da30bc48b8d622210b4b26d91510a956
https://research.wur.nl/en/publications/determination-of-specific-and-non-specific-protein-protein-intera
https://research.wur.nl/en/publications/determination-of-specific-and-non-specific-protein-protein-intera
Publikováno v:
Soft Matter Systems for Biomedical Applications
Springer Proceedings in Physics ISBN: 9783030809232
Soft Matter Systems for Biomedical Applications. Cham: Springer
Springer Proceedings in Physics ISBN: 9783030809232
Soft Matter Systems for Biomedical Applications. Cham: Springer
The increasing knowledge about natural functional fibrils has triggered the interest in synthetic or engineered fibrils. Naturally occurring amyloid fibrils (functional and pathogenic) have been analyzed for many years at different structural levels.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a803f96c361f180b5361f08fa81c3fd
https://doi.org/10.1007/978-3-030-80924-9_11
https://doi.org/10.1007/978-3-030-80924-9_11
Autor:
Vanessa Lautenbach, Laura Fitzner, Uwe Jandt, Elena Kempf, Timon R. Heyn, Rebekka Biedendieck, Eva Scheidler, Krzysztof Lewiński, Jonas Lohr, Dieter Jahn, Anja Heyse, J.I. Loch, Julia K. Keppler, Karin Schwarz, Maximilian J. Uttinger, Gabriele Günther, Christian Lübbert, Wolfgang Peukert, Stephan Drusch, Ulrich Kulozik, Jan Hendrik Grosch, Helena Kieserling, Rainer Krull
Publikováno v:
Food Hydrocolloids, 110
Food Hydrocolloids 110 (2021)
Food Hydrocolloids (110): 106132 (2021-01)
Food hydrocolloids 110, 106132 (2021). doi:10.1016/j.foodhyd.2020.106132
Food Hydrocolloids 110 (2021)
Food Hydrocolloids (110): 106132 (2021-01)
Food hydrocolloids 110, 106132 (2021). doi:10.1016/j.foodhyd.2020.106132
Food hydrocolloids 110, 106132 (2021). doi:10.1016/j.foodhyd.2020.106132
Published by Elsevier, Amsterdam
Published by Elsevier, Amsterdam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2f58c4d7e3fc8464cb795b0cd9b255c
https://research.wur.nl/en/publications/towards-recombinantly-produced-milk-proteins-physicochemical-and-
https://research.wur.nl/en/publications/towards-recombinantly-produced-milk-proteins-physicochemical-and-
Autor:
Arno Kwade, Julia K. Keppler, Wolfgang Peukert, Karin Schwarz, Maximilian J. Uttinger, Timon R. Heyn
Publikováno v:
Journal of Food Engineering, 311
Journal of Food Engineering 311 (2021)
Journal of Food Engineering 311 (2021)
Whey protein fibrils are excellent emulsifiers. However, the emulsification process significantly alters the size of the aggregates and thus their functionality. It is not yet known how strongly the disperse phase (oil) contributes to the size change
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ec5b51052ade43f8c301cc650a85718
https://research.wur.nl/en/publications/whey-protein-amyloid-aggregates-in-oil-water-systems-the-process-
https://research.wur.nl/en/publications/whey-protein-amyloid-aggregates-in-oil-water-systems-the-process-
Autor:
Ingo Kampen, Julia K. Keppler, Jacqueline Lux, Karin Schwarz, Anja Steffen-Heins, Timon R. Heyn
Publikováno v:
Food Hydrocolloids, 112
Food Hydrocolloids 112 (2021)
Food Hydrocolloids 112 (2021)
Site-directed spin labeling (SDSL) of the natural food protein β-lactoglobulin (β-lg) was established with the aim of characterizing amyloid aggregation while explicitly avoiding the usual manipulation of primary protein structure. For its successf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fff16bdb6e45056ce10ef768aec53de
Autor:
Uwe Jandt, Simon E. Wawra, Wolfgang Peukert, Timon R. Heyn, Julia K. Keppler, Bettina Winzer, Maximilian J. Uttinger
Publikováno v:
European Biophysics Journal 49 (8): 745-760 (2020)
European Biophysics Journal 49 (2020)
European Biophysics Journal, 49, 745-760
European Biophysics Journal
European Biophysics Journal 49 (2020)
European Biophysics Journal, 49, 745-760
European Biophysics Journal
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 frag
Autor:
Timon R. Heyn, Christine Selhuber-Unkel, Hendrikje R. Neumann, Arno Kwade, Julian K. Mayer, Julia K. Keppler, Karin Schwarz
Publikováno v:
Journal of Food Engineering, 283
Journal of Food Engineering 283 (2020)
Journal of Food Engineering 283 (2020)
This study identifies critical factor combinations of pH, temperature, stirring speed, protein and ion concentration that specifically affect the lag-, and growth phase of beta-lactoglobulin amyloid aggregation and provides information on how, when a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32f2504fb727254c9e5f1634f8d53510
https://research.wur.nl/en/publications/the-threshold-of-amyloid-aggregation-of-beta-lactoglobulin-releva
https://research.wur.nl/en/publications/the-threshold-of-amyloid-aggregation-of-beta-lactoglobulin-releva
Autor:
L.J.G. Hoppenreijs, Remko M. Boom, Julia K. Keppler, Timon R. Heyn, Karin Schwarz, A.J. van der Goot, T. Ruhmlieb, Laura Fitzner, Anja Steffen-Heins, K. Schild
Publikováno v:
Food Hydrocolloids 124 (2022) Part A
Food Hydrocolloids, 124(Part A)
Food Hydrocolloids, 124(Part A)
Background: Depending on environmental conditions, almost all proteins can form amyloid and amyloid-like aggregates that have unique functional properties. This opens numerous applications for designed aggregates in materials, medical and food applic