Secretory and extracellular production of recombinant proteins using Escherichia coli

By J. Choi, S. Y. Lee. Applied Microbiology and Biotechnology, 2004

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Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems (2006, methodology): “The following signal peptides are in use for secretion of heterologously expressed proteins: Lpp, LamB, LTB, MalE, OmpA, OmpC, OmpF, OmpT, PelB, PhoA, PhoE, SpA, and Tat signal peptides (reviewed in Choi and Lee 2004; Mergulhao et al. 2005).”
Recombinant protein expression in Escherichia coli: advances and challenges (2014, methodology): “The signal peptides of the following proteins are widely used for secretion: Lpp, LamB, LTB, MalE, OmpA, OmpC, OmpF, OmpT, PelB, PhoA, PhoE, or SpA (Choi and Lee, 2004).”
Production of recombinant proteins by high cell density culture of Escherichia coli (2006, methodology): “As secretory production system can be much more beneficial for the production of some proteins (e.g. those proteins requiring disulfide bond formation), researches are underway to achieve successful secretory production in a HCDC mode (Choi and Lee, 2004; Choi et al., 2000; Yim et al., 2001).”
Production of recombinant proteins by microbes and higher organisms. (2009, background): “…the growthmedium; (viii) addition of a fusion partner; (ix) expression of a fragment of the protein; and (x) in vitro denaturation and refolding of the protein (Swartz, 2001; Choi and Lee, 2004; Mergulhao et al., 2005; Shiloach and Fass, 2005; Maldonado et al., 2007; Chou, 2007; Wong et al., 2008).”