Recombinant protein solubility—does more mean better?

N Gonzalez-Montalban, E Garcia-Fruitos… - Nature …, 2007 - nature.com
Since the inception of recombinant DNA technology, maximizing the solubility of a
heterologous protein has been the goal of large-scale biomanufacture1. In bacterial cell …

[HTML][HTML] High-yield production of functional soluble single-domain antibodies in the cytoplasm of Escherichia coli

K Zarschler, S Witecy, F Kapplusch, C Foerster… - Microbial cell …, 2013 - Springer
Background For their application in the area of diagnosis and therapy, single-domain
antibodies (sdAbs) offer multiple advantages over conventional antibodies and fragments …

[HTML][HTML] Quality control of inclusion bodies in Escherichia coli

B Jürgen, A Breitenstein, V Urlacher, K Büttner… - Microbial cell …, 2010 - Springer
Abstract Background Bacterial inclusion bodies (IBs) are key intermediates for protein
production. Their quality affects the refolding yield and further purification. Recent functional …

[HTML][HTML] Strategic optimization of conditions for the solubilization of GST-tagged amphipathic helix-containing ciliary proteins overexpressed as inclusion bodies in E …

AA Shendge, JS D'Souza - Microbial cell factories, 2022 - Springer
Expression of affinity-tagged recombinant proteins for crystallography, protein–protein
interaction, antibody generation, therapeutic applications, etc. mandates the generation of …

[HTML][HTML] Engineering inclusion bodies for non denaturing extraction of functional proteins

Š Peternel, J Grdadolnik, V Gaberc-Porekar… - Microbial cell …, 2008 - Springer
Background For a long time IBs were considered to be inactive deposits of accumulated
target proteins. In our previous studies, we discovered IBs containing a high percentage of …

[HTML][HTML] Protein aggregation as bacterial inclusion bodies is reversible

MM Carrió, A Villaverde - FEBS letters, 2001 - Elsevier
Inclusion bodies are refractile, intracellular protein aggregates usually observed in bacteria
upon targeted gene overexpression. Since their occurrence has a major economical impact …

Proteome‐based identification of fusion partner for high‐level extracellular production of recombinant proteins in Escherichia coli

ZG Qian, XX Xia, JH Choi… - Biotechnology and …, 2008 - Wiley Online Library
Extracellular production of recombinant proteins in Escherichia coli has several advantages
over cytoplasmic or periplasmic production. However, nonpathogenic laboratory strains of E …

Catalytically-active inclusion bodies—Carrier-free protein immobilizates for application in biotechnology and biomedicine

U Krauss, VD Jäger, M Diener, M Pohl… - Journal of biotechnology, 2017 - Elsevier
Bacterial inclusion bodies (IBs) consist of unfolded protein aggregates and represent
inactive waste products often accumulating during heterologous overexpression of …

[HTML][HTML] Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region

K Mirzadeh, PJ Shilling, R Elfageih, AJ Cumming… - Microbial Cell …, 2020 - Springer
Background Recombinant proteins are often engineered with an N-terminal signal peptide,
which facilitates their secretion to the oxidising environment of the periplasm (gram-negative …

[HTML][HTML] A novel Ecotin-Ubiquitin-Tag (ECUT) for efficient, soluble peptide production in the periplasm of Escherichia coli

M Paal, T Heel, R Schneider, B Auer - Microbial cell factories, 2009 - Springer
Background Many protocols for recombinant production of peptides and proteins include
secretion into the periplasmic space of Escherichia coli, as they may not properly fold in the …