Evidence map›Paper›PMID 38573344›Full record

ArticleAnalytical and bioanalytical chemistry2024

Online monitoring of protein refolding in inclusion body processing using intrinsic fluorescence.

Chika Linda Igwe, Don Fabian Müller, Florian Gisperg, Jan Niklas Pauk, Matthias Kierein, Mohamed Elshazly, Robert Klausser, Julian Kopp, Oliver Spadiut, Eva Přáda Brichtová

Abstract read
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In one paragraph

Article in Analytical and bioanalytical chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Chika Linda Igwe *Competence Center CHASE GmbH, Hafenstraße 47-51, Linz, 4020, Austria.
Don Fabian Müller *Research Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Florian GispergResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Jan Niklas PaukCompetence Center CHASE GmbH, Hafenstraße 47-51, Linz, 4020, Austria.
Matthias KiereinResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Mohamed ElshazlyResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Robert KlausserResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Julian KoppResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Oliver SpadiutResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria.
Eva Přáda BrichtováResearch Area Biochemical Engineering, Institute of Chemical, Environmental and Bioscience Engineering, Technische Universität Wien, Gumpendorferstraße 1A, Vienna, 1060, Austria. eva.prada@tuwien.ac.at.ORCID http://orcid.org/0000-0001-9888-6185

Funding

Austrian Research Promotion Agency (FFG) COMET Centre CHASEChristian Doppler Forschungsgesellschaft (CDG) and Boehringer Ingelheim RCV CD-Labor für Inclusion Body Prozessierung 4.0
6 · The paper itself

Abstract

Inclusion bodies (IBs) are protein aggregates formed as a result of overexpression of recombinant protein in E. coli. The formation of IBs is a valuable strategy of recombinant protein production despite the need for additional processing steps, i.e., isolation, solubilization and refolding. Industrial process development of protein refolding is a labor-intensive task based largely on empirical approaches rather than knowledge-driven strategies. A prerequisite for knowledge-driven process development is a reliable monitoring strategy. This work explores the potential of intrinsic tryptophan and tyrosine fluorescence for real-time and in situ monitoring of protein refolding. In contrast to commonly established process analytical technology (PAT), this technique showed high sensitivity with reproducible measurements for protein concentrations down to 0.01 g L

Indexed as

Inclusion BodiesProtein RefoldingSpectrometry, FluorescenceEscherichia coliFluorescenceProtein FoldingRecombinant ProteinsTryptophanTyrosineRecombinant ProteinsTryptophanTyrosineInclusion bodyMechanistic modelProcess analytical technology (PAT)Protein refoldingTryptophan and tyrosine fluorescence

Identifiers

PMID38573344
PMCPMC11045631

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LicenceCC BY
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.