Table 1 Production of purified BLIP using various expression systems
Expression host | Mode of expression | Purification steps involved | Yield of BLIP | References |
|---|---|---|---|---|
Streptomyces clavuligerus (Native host) | Secretory protein with BLIP’s own signal peptide | (1) Ammonium sulfate precipitation (2) Gel filtration (3) Ion exchange chromatography | BLIP represented 10% of the total exocellular proteins in S. clavuligerus 1.24 mg from 37.4 mg total protein of culture filtrate | Doran et al. (1990) |
Streptomyces lividans | Secretory protein with native BLIP signal peptide | Not purified | Amount in culture filtrate was 12-fold lower than that in Streptomyces clavuligerus | Paradkar et al. (1994) |
Escherichia coli | Intracellular fusion protein with maltose-binding protein | Not reported | Not reported | Rudgers and Palzkill (1999) |
Intracellular protein that formed inclusion bodies | (1) Ion exchange chromatography (2) Gel filtration | ~ 1.6–4.2 mg/L culture | Albeck and Schreiber (1999) | |
Intracellular 6×His-tag protein that formed inclusion bodies | Metal affinity chromatography | 2.2 mg/L culture | Hu et al. (2016) | |
Intracellular 6×His-tag protein with β-lactamase signal peptide that was transported to the periplasmic space | Metal affinity chromatography | ~ 0. 25 mg/L culture | Petrosino et al. (1999) | |
Intracellular protein with native S. clavuligeris signal peptide that was transported to the periplasmic space | (1) Ion exchange chromatography (2) Gel filtration | 0.5 mg/L culture | Reyonlds et al. (2006) | |
Bacillus subtilis | Secretory protein with native BLIP signal peptide | (1) Ammonium sulfate precipitation (2) Ion exchange chromatography | ~ 3.5 mg/L culture | Liu et al. (2004) |
Pichia pastoris | Secretory protein with α-factor mating signal peptide | Not purified | ~ 300 mg/L culture | This study |