Recombinant expression of hydroxylated human collagen in Escherichia coli

Collagen is the most abundant protein in the human body and thereby a structural protein of considerable biotechnological interest. The complex maturation process of collagen, including essential post-translational modifications such as prolyl and lysyl hydroxylation, has precluded large-scale produ...

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Veröffentlicht in:	Applied microbiology and biotechnology 2014-05, Vol.98 (10), p.4445-4455
Hauptverfasser:	Rutschmann, Christoph, Baumann, Stephan, Cabalzar, Jürg, Luther, Kelvin B, Hennet, Thierry
Format:	Artikel
Sprache:	eng
Schlagworte:	biocompatibility biocompatible materials Biomaterials Biomedical and Life Sciences Biomedical engineering Biomedical materials Biotechnologically Relevant Enzymes and Proteins Biotechnology Collagen Collagen Type III - genetics Collagen Type III - metabolism E coli endothelial cells engineering Enzyme Stability Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism extracellular matrix genes Genetic aspects Humans Hydroxylation hydroxylysine Hydroxyproline Life Sciences Mass Spectrometry Metabolic Engineering - methods Microbial Genetics and Genomics Microbiology Mimiviridae - enzymology Mimiviridae - genetics Mimivirus Molecular Sequence Data Peptides Post-translational modification Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - genetics Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - metabolism Prolyl Hydroxylases - genetics Prolyl Hydroxylases - metabolism Protein Conformation Protein expression Protein Processing, Post-Translational Proteins Recombinant proteins Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Analysis, DNA Studies Temperature thermal stability Viruses
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