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The use of a surface active agent in the protection of a fusion protein during bioprocessing
The bioprocessing of a fusion protein is characterised by low yields and at a series of recovery and purification stages that leads to an overall 90% loss. Much of this apparent loss is due to the denaturation of a protein, missing a vital affinity ligand. However, there is evidence of the protectio...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6334174/ https://www.ncbi.nlm.nih.gov/pubmed/30102764 http://dx.doi.org/10.1002/bit.26817 |
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author | Blas, Peter Tolner, Berend Ward, John Chester, Kerry Hoare, Mike |
author_facet | Blas, Peter Tolner, Berend Ward, John Chester, Kerry Hoare, Mike |
author_sort | Blas, Peter |
collection | PubMed |
description | The bioprocessing of a fusion protein is characterised by low yields and at a series of recovery and purification stages that leads to an overall 90% loss. Much of this apparent loss is due to the denaturation of a protein, missing a vital affinity ligand. However, there is evidence of the protection of degradation products which occurs in the presence of shear plus air/liquid interfaces. This study seeks out to characterise the loss and use ultra‐scale‐down studies to predict its occurrence and hence shows these may be diminished by the use of protective reagents such as Pluronic F68. |
format | Online Article Text |
id | pubmed-6334174 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-63341742019-01-23 The use of a surface active agent in the protection of a fusion protein during bioprocessing Blas, Peter Tolner, Berend Ward, John Chester, Kerry Hoare, Mike Biotechnol Bioeng ARTICLES The bioprocessing of a fusion protein is characterised by low yields and at a series of recovery and purification stages that leads to an overall 90% loss. Much of this apparent loss is due to the denaturation of a protein, missing a vital affinity ligand. However, there is evidence of the protection of degradation products which occurs in the presence of shear plus air/liquid interfaces. This study seeks out to characterise the loss and use ultra‐scale‐down studies to predict its occurrence and hence shows these may be diminished by the use of protective reagents such as Pluronic F68. John Wiley and Sons Inc. 2018-09-08 2018-11 /pmc/articles/PMC6334174/ /pubmed/30102764 http://dx.doi.org/10.1002/bit.26817 Text en © 2018 The Authors. Biotechnology and Bioengineering Published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | ARTICLES Blas, Peter Tolner, Berend Ward, John Chester, Kerry Hoare, Mike The use of a surface active agent in the protection of a fusion protein during bioprocessing |
title | The use of a surface active agent in the protection of a fusion protein during bioprocessing |
title_full | The use of a surface active agent in the protection of a fusion protein during bioprocessing |
title_fullStr | The use of a surface active agent in the protection of a fusion protein during bioprocessing |
title_full_unstemmed | The use of a surface active agent in the protection of a fusion protein during bioprocessing |
title_short | The use of a surface active agent in the protection of a fusion protein during bioprocessing |
title_sort | use of a surface active agent in the protection of a fusion protein during bioprocessing |
topic | ARTICLES |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6334174/ https://www.ncbi.nlm.nih.gov/pubmed/30102764 http://dx.doi.org/10.1002/bit.26817 |
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