Enhancement of stability of recombinant streptokinase by intracellular expression and single step purification by hydrophobic interaction chromatography

Biochemical Engineering Journal

Volumn 39, Issue 1, 2008, Pages 84-90

  Balagurunathan, Balaji ^a   Ramchandra, Narkhede Sachin ^a   Jayaraman, Guhan ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY MADRAS   (India)

Author keywords

Escherichia coli; Hydrophobic interaction chromatography; Intracellular expression; Recombinant streptokinase; Single step purification

Indexed keywords

BIOACTIVITY; CHROMATOGRAPHIC ANALYSIS; ESCHERICHIA COLI; GENE EXPRESSION; PROTEINS; SOLUBILITY;

HYDROPHOBIC INTERACTION CHROMATOGRAPHY; INTRACELLULAR EXPRESSION; RECOMBINANT STREPTOKINASE; SINGLE STEP PURIFICATION;

ENZYME ACTIVITY;

PROTEIN; STREPTOKINASE;

ARTICLE; BIOMASS; CHROMATOGRAPHY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CYTOPLASM; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STABILITY; SOLUBILITY;

ESCHERICHIA COLI;

EID: 43049124167     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2007.08.021     Document Type: Article

References (36)

1. Tillett W.S., and Garner R.L. The fibrinolytic activity of hemolytic streptococci. J. Exp. Med. 58 (1933) 485-502
2. World Health Organization, The WHO Model List of Essential Medicines, 14th ed., March 2005, http://whqlibdoc.who.int/hq/2005/a87017_eng.pdf (accessed on 15th September 2006).
3. Hermentin P., Cuesta-Linker T., Weisse J., Schmidt K.H., Knorst M., Scheld M., and Thimme M. Comparative analysis of the activity and content of different streptokinase preparations. Eur. Heart. J. 26 (2005) 933-940
4. Couto L.T., Donato J.L., and de Nucci G. Analysis of five streptokinase formulations using the euglobulin lysis test and the plasminogen activation assay. Braz. J. Med. Biol. Res. 37 (2004) 1889-1894
5. Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10 (1999) 411-421
6. Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 11 (2004) 1399-1408
7. Clark E.D.B. Refolding of recombinant proteins. Curr. Opin. Biotechnol. 9 (1998) 157-163
8. Ignatova Z., Enfors S.O., Hobbie M., Taruttis S., Vogt C., and Kasche V. The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli. Enzyme Microbiol. Technol. 26 (2000) 165-170
9. Enfors S.O. Control of in vivo proteolysis in the production of recombinant proteins. Trends Biotechnol. 10 (1992) 310-315
10. Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30 (1996) 465-506
11. Liu Y., Zhao T.J., Yan Y.B., and Zhou H.M. Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Prot. Expr. Purif. 44 (2005) 155-161
12. Sorenson H.P., and Mortensen K.K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115 (2005) 113-128
13. Sorenson H.P., and Mortensen K.K. Soluble expression of recombinant streptokinase in the cytoplasm of Escherichia coli. Microbiol. Cell. Fac. 4 (2005) 1
14. Malke H., and Ferretti J.J. Streptokinase: cloning, expression and excretion by Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 81 (1984) 3557-3561
15. Avilan L., Yarzabal A., Jurgensen C., Bastidas M., Cruz J., and Puig J. Cloning, expression and purification of recombinant streptokinase: partial characterization of the protein expressed in Escherichia coli. Braz. J. Med. Biol. Res. 30 (1997) 1427-1430
16. Estrada M.P., Hernandez L., Perez A., Rodriguez P., Serrano R., and Rubier A.R. High-level expression of streptokinase in Escherichia coli. Biotechnology 10 (1992) 1138-1142
17. Goyal D., Sahoo D.K., and Sahni G. Hydrophobic interaction expanded bed adsorption chromatography (HI-EBAC) based facile purification of recombinant streptokinase from E. coli inclusion bodies. J. Chromatogr. B 850 (2007) 384-391
18. Ko J.H., Park D.K., Kim I.C., Lee S.H., and Byun S.M. High-level expression and secretion of streptokinase in Escherichia coli. Biotechnol. Lett. 17 (1995) 1019-1024
19. Lee S.H., Kim I.C., Bae K.H., and Byun S.M. Enhanced production and secretion of streptokinase into extracellular medium in Escherichia coli by removal of 13 N-terminal amino acids. Biotechnol. Lett. 19 (1997) 151-154
20. Perez N., Urrutia E., Camino J., Orta D.R., Torres Y., and Martinez Y. Hydrophobic interaction chromatography applied to purification of recombinant streptokinase. Biotechnology 10 (1998) 174-177
21. Pratap J., and Dikshit K.L. Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction. Mol. Gen. Genet. 258 (1998) 326-333
22. Pupo E., Baghbaderani B.A., Lugo V., Fernandez J., Paez R., and Torrens I. Two streptokinase genes are expressed with different solubility in Escherichia coli W3110. Biotechnol. Lett. 21 (1999) 1119-1123
23. Ramalingam S., Gautam P., Mukherjee K.J., and Jayaraman G. Effect of post-induction feed strategies on secretory production of recombinant streptokinase in Escherichia coli. Biochem. Eng. J. 33 (2007) 34-41
24. Yazdani S.S., and Mukherjee K.J. Overexpression of streptokinase using a fed-batch strategy. Biotechnol. Lett. 20 (1998) 923-927
25. Yazdani S.S., and Mukherjee K.J. Continuous culture studies on the stability and expression of recombinant streptokinase in Escherichia coli. Bioproc. Biosyst. Eng. 24 (2002) 341-346
26. Zhang X.W., Sun T., Huang X.N., Liu X., Gu D.X., and Tang Z.Q. Recombinant streptokinase production by fed-batch cultivation of Escherichia coli. Enzyme Microb. Technol. 24 (1999) 647-650
27. Hong S.H., Toyama M., Maret W., and Murooka Y. High yield expression and single step purification of Human Thionein/Metallothionein. Prot. Expr. Purif. 21 (2001) 243-250
28. Khushoo A., Pal Y., Singh B.N., and Mukherjee K.J. Extracellular expression and single step purification of recombinant Escherichia coli l-asparaginase II. Prot. Expr. Purif. 38 (2004) 29-36
29. Wang F., He X.W., Yan H.L., Huang J.J., Zhang Y., Jiang L., Gao Y.J., and Sun S.H. Non-fusion expression in Escherichia coli: single-step purification of recombinant human annexin A5 for detection of apoptosis. Prot. Expr. Purif. 45 (2006) 80-87
30. Sambrook J., and Russel D.W. Molecular cloning: a laboratory manual. 3rd ed. (2001), Cold Spring Harbor Laboratory Press
31. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
32. Switzer III R.C., Merrill C.R., and Shifrin S. A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal. Biochem. 98 (1979) 231-237
33. Sammons D.W., Adams L.D., and Nishizawa E.E. Ultra sensitive silver based color staining of polypeptides in polyacrylamide gels. Electrophoresis 2 (1981) 135-141
34. Parhami-Seren B., Krudysz J., and Tsantili P. Affinity panning of peptide libraries using anti-streptokinase monoclonal antibodies: selection of an inhibitor of plasminogen active site. J. Immunol. Methods 267 (2002) 185-198
35. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Biochemistry 72 (1976) 248-254
36. Subramanian G. Bioseparation and Bioprocessing-A Handbook 1 (1998), Wiley-VCH