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020 _a9783031631641
_9978-3-031-63164-1
024 7 _a10.1007/978-3-031-63164-1
_2doi
050 4 _aTP1-1185
072 7 _aTDC
_2bicssc
072 7 _aSCI013060
_2bisacsh
072 7 _aTDC
_2thema
245 1 0 _aDispersity, Structure and Phase Changes of Proteins and Bio Agglomerates in Biotechnological Processes
_h[electronic resource] /
_cedited by Arno Kwade, Ingo Kampen.
250 _a1st ed. 2024.
264 1 _aCham :
_bSpringer Nature Switzerland :
_bImprint: Springer,
_c2024.
300 _aIX, 547 p. 276 illus., 165 illus. in color.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
505 0 _a1. Correlation of structure and properties of enzyme crystals in consideration of downstream processing and formulation -- 2. Multiscale Model-Based Investigation of Functional Macromolecular Agglomerates for Biotechnological Applications -- 3. Modeling-based Monitoring and Control of Protein Crystallization in Bioprocesses -- 4. Changes in structure, dispersity and phase behavior of proteins: The virus-like particles in the presence of nucleic acids.
520 _aThis book serves as a comprehensive summary of the priority program SPP 1934, which focused on understanding the dispersity, structure, and phase changes of proteins and bio-agglomerates in biotechnological processes. Through contributions from various research groups, the program explored how sensitive proteins and bio-agglomerates are affected by the process environment during fermentation, downstream processing, and formulation. It investigated these effects across three size scales: microscale, encompassing single proteins, clusters, crystals, and virus-like particles; mesoscale, focusing on cells and cell clusters; and macroscale, examining overall process dynamics. The main objective was to enhance biotechnological process chains by elucidating the mechanical, thermal, and chemical stresses that impact protein and bio-agglomerate structures. By gaining insights into these stressors, the program aimed to enable precise control measures to mitigate denaturation and unfavorable growth of proteins and cells. This compilation seeks to contribute to the optimization of biotechnological processes, facilitating advancements in various industries.
650 0 _aChemistry, Technical.
_969610
650 0 _aProteins .
_970651
650 1 4 _aIndustrial Chemistry.
_969611
650 2 4 _aProtein Biochemistry.
_971768
700 1 _aKwade, Arno.
_eeditor.
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
_985059
700 1 _aKampen, Ingo.
_eeditor.
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
_985060
710 2 _aSpringerLink (Online service)
773 0 _tSpringer Nature eBook
776 0 8 _iPrinted edition:
_z9783031631634
776 0 8 _iPrinted edition:
_z9783031631658
776 0 8 _iPrinted edition:
_z9783031631665
856 4 0 _uhttps://doi.org/10.1007/978-3-031-63164-1
912 _aZDB-2-CMS
912 _aZDB-2-SXC
999 _c63738
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