MAXIMIZING THE EXPRESSION OF RECOMBINANT KRINGLE-1 (STREPTOKINASE) SYNTHESIZED IN ESCHERICHIA-COLI - INFLUENCE OF CULTURE AND INDUCTION CONDITIONS

We examined the influence of culture conditions on the production of t he recombinant fused protein Kringle 1 (Streptokinase) (K1(SK)) expres sed in E. coil under the control of the lpp-lac promoter. The growth a nd the protein production were severely inhibited at glucose concentra tions higher than 5 g/L. The highest yield of K1(SK) from the soluble extract was obtained using synthetic medium. Concentrations of inducer between 0.1 and 1 mM of IPTG did not significantly affect the product ion level of K1(SK) or the final cell density. Under optimal condition s the K1(SK) protein was expressed in an intracellular soluble form at about 3-4% of the total cellular protein.