[Recombinant protein production in Escherichia coli].
Growing needs for efficient recombinant production pose new challenges; starting from cell growth optimization under overexpression conditions, improving vectors, gene and protein sequence to suit them to protein biosynthesis machinery of the host, through extending the knowledge of protein folding, fusion protein construction, and coexpression systems, to improvements in protein purification and renaturation technologies. Hitherto Escherichia coli is the most defined and the cheapest protein biosynthesis system. With its wealth of available mutants tested is the best suited to economically test new gene constructs and to scale up the recombinant protein production.
Nuc
Przemysław
P
Uniwersytet im. Adama Mickiewicza, Instytut Biologii Molekularnej i Biotechnologii, Poznán. przem@amu.edu.pl
Nuc
Katarzyna
K
D001483:Base Sequence / Q000235:genetics; D002846:Chromatography, Affinity / Q000295:instrumentation / Q000379:methods; D003470:Culture Media; D004926:Escherichia coli / Q000502:physiology*; D005822:Genetic Vectors / Q000235:genetics / Q000378:metabolism*; D002479:Inclusion Bodies / Q000737:chemistry; D019897:Periplasm / Q000737:chemistry; D010957:Plasmids / Q000096:biosynthesis; D011401:Promoter Regions, Genetic / Q000235:genetics; D014176:Protein Biosynthesis / Q000502:physiology*; D017510:Protein Folding; D020673:Protein Renaturation; D020871:RNA Stability; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000191:economics / Q000302:isolation & purification*; D012107:Research Design
D003470:Culture Media; D011994:Recombinant Proteins