title: Recombinant protein secretion in Escherichia coli.
abstract: The secretory production of recombinant proteins by the Gram-negative bacterium Escherichia coli has several advantages over intracellular production as inclusion bodies. In most cases, targeting protein to the periplasmic space or to the culture medium facilitates downstream processing, folding, and in vivo stability, enabling the production of soluble and biologically active proteins at a reduced process cost. This review presents several strategies that can be used for recombinant protein secretion in E. coli and discusses their advantages and limitations depending on the characteristics of the target protein to be produced.
authors.affiliation: Centro de Engenharia Biológica e Química, Instituto Superior Técnico, Av. Rovisco Pais, Lisbon 1049-001, Portugal. filipem@alfa.ist.utl.pt
authors.forename: F J M
authors.initials: FJ
authors.lastname: Mergulhão
authors.forename: D K
authors.initials: DK
authors.lastname: Summers
authors.forename: G A
authors.initials: GA
authors.lastname: Monteiro
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins