Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins

Table 2 Production yield of purified recombinant Trx-TB10.4, Trx-Ag85B (chimeric and single antigens, after proteolytic cleavage), and His- full 2 by E. coli cells grown at flask and bioreactor scales

Protein	Growth conditions	Biomass at the harvest time^a(g/L)	Pure chimeric protein^b (mg/L)	Pure mature protein (mg/L)
Trx-TB10.4	Flasks	4.8	12	4^c
	Bioreactor	8.5	80	25^c
Trx-Ag85B	Flasks	10.5	9	4.7^c
	Bioreactor	19.5	30	16^c
His-full 2	Flasks	6.5	/	0.5
	Bioreactor	6.5	/	2.5

^agrams of E. coli cells (wet weight) per liter of cultivation broth at the harvest time.
^bmilligrams of protein obtained upon purification by nickel-affinity chromatography per liter of cultivation broth.
^cmilligrams of protein obtained upon proteolytic cleavage and separation by nickel-affinity chromatography per liter of cultivation broth.

ISSN: 1475-2859