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|a UAMI
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|a Gädke, Johannes.
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|a In situ-downstream processing of recombinant histidine-tagged proteins from cultivations of Bacillus megaterium.
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|a Göttingen :
|b Cuvillier Verlag,
|c 2017.
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| 300 |
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|a 1 online resource (129 pages)
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|a Schriftenreihe des Institutes für Bioverfahrenstechnik der Technischen Universität Braunschweig ;
|v v. 79
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|a Print version record.
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|a Danksagung; Summary; Zusammenfassung; Index; 1 Introduction and aims of the thesis; 2 Current state of research; 3 Materials and methods; 4 Results and discussion; 5 Conclusion and outlook; 6 Literature.
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| 504 |
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|a Includes bibliographical references.
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|a eBooks on EBSCOhost
|b EBSCO eBook Subscription Academic Collection - Worldwide
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|a ProQuest Ebook Central
|b Ebook Central Academic Complete
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| 650 |
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|a Bacillus (Bacteria)
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| 650 |
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|a Bacillus megaterium.
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| 650 |
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6 |
|a Bacillus (Bactéries)
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| 650 |
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|a Bacillus megaterium.
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| 650 |
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|a Bacillus (Bacteria)
|2 fast
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| 650 |
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|a Bacillus megaterium
|2 fast
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|i Print version:
|a Gädke, Johannes.
|t In situ-downstream processing of recombinant histidine-tagged proteins from cultivations of Bacillus megaterium.
|d Göttingen : Cuvillier Verlag, ©2017
|z 9783736995512
|
| 830 |
|
0 |
|a Schriftenreihe des Institutes für Bioverfahrenstechnik der Technischen Universität Braunschweig.
|
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4 |
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|u https://ebookcentral.uam.elogim.com/lib/uam-ebooks/detail.action?docID=5022934
|z Texto completo
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| 880 |
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|6 520-00/(S
|a Purification of (recombinant) proteins for industrial and pharmaceutical use is accompanied by high costs and difficulties in the scale-up with the necessity of many purification steps. This thesis demonstrates the use of functionalized superparamagnetic iron oxide nanoparticles for the purification of recombinant histidine-tagged proteins directly from a growing culture of the gram-positive bacterium Bacillus megaterium. The separation was performed using commercial hand held magnets. Regenerability and reusability are shown in shake flask scale. Automation of the process is demonstrated at lab scale bioreactors using two model proteins, Protein A and the antibody fragment α-Lysozyme D1.3scFv. The process demonstrates a quick and easy way to yield a product of high purity within a short period of time.
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