Enhanced enzyme activities of inclusion bodies of recombinant β-galactosidase via the addition of inducer analog after L-arabinose induction in the araBAD promoter system of Escherichia coli

Journal of Microbiology and Biotechnology

Volumn 18, Issue 3, 2008, Pages 434-442

  Jung, Kyung Hwan ^a  

^a Chungju National University   (South Korea)

Author keywords

galactosidase; Inclusion body; Inducer analog; Partial repression

Indexed keywords

ARABINOSE; BETA GALACTOSIDASE; FUCOSE; RECOMBINANT BETA GALACTOSIDASE; RECOMBINANT ENZYME; ESCHERICHIA COLI PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; BIOCATALYST; BIOPROCESS; CELL INCLUSION; CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INDUCTION; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; PROMOTER REGION; PROTEIN CARBOHYDRATE INTERACTION; STRUCTURAL GENE; TRANSCRIPTION REGULATION; CHEMISTRY; FERMENTATION; GENE EXPRESSION REGULATION; GENETICS; INFRARED SPECTROSCOPY; METABOLISM;

ESCHERICHIA COLI;

ARABINOSE; BETA-GALACTOSIDASE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FERMENTATION; FUCOSE; GENE EXPRESSION REGULATION, BACTERIAL; INCLUSION BODIES; PROMOTER REGIONS (GENETICS); RECOMBINANT PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 46749083949     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: None     Document Type: Article

References (30)

1. Ami, D., L. Bonecchi, S. Cali, G. Orsini, G. Tonon, and S. M. Doglia. 2003. FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim. Biophys. Acta 1624: 6-10.
2. Ami, D., A. Natalello, P. Gatti-Lafranconi, M. Lotti, and S. M. Doglia. 2005. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy FEBS Lett 579: 3433-3436.
3. Bramhachari, P. V., P. B. Kavikishor, R. Ramadevi, R. Kumar, B. R. Rao, and S. K. Dubey. 2007. Isolation and characterization of mucous exopolysaccharide (EPS) produced by Vibrio furnissii strain VBOS3. J. Microbiol. Biotechnol. 17: 44-51.
4. Bukau, B., J. Weissman, and A. Horwich. 2006. Molecular chaperones and protein quality control. Cell 125: 443-451.
5. Carrio, M., N. González-Montalbán, A. Vera, A. Villaverde, and S. Ventura. 2005. Amyloid-like properties of bacterial inclusion bodies. J. Mol. Biol. 347: 1025-1037.
6. Davis, G. D., C. Elisee, D. M. Newham, and R. G Harrison. 1999. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 65: 382-398.
7. de Groot, N. S. and S. Ventura. 2006. Effect of temperature on protein quality in bacterial inclusion bodies. FEBS Lett. 580: 6471-6476.
8. de Groot, N. S. and S. Ventura. 2006. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J. Biotechnol. 125: 110-113.
9. Duetz, W. A., L. Rüedi, R. Hermann, K. O'Connor, J. Büchs, and B. Witholt. 2000. Methods for intense aeration, growth, storage, and replication of bacterial strains in microtiter plates. Appl. Environ. Microbiol. 66: 2641-2646.
10. Garcia-Fruitos, E., M. M. Carrio, A. Aris, and A. Villaverde. 2005. Folding of a misfolding-prone β-galactosidase in absence of DnaK. Biotechnol. Bioeng. 90: 869-875.
11. García-Fruitós, E., N. González-Montalbán M. Morell, A. Vera, R. M. Ferraz, A. Arís, S. Ventura, and A. Villaverde. 2005. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb. Cell Fact. 4: 27.
12. González-Montalbán, N., E. García-Fruitós, S. Ventura, A. Arís, and A. Villaverde. 2006. The chaperone DnaK controls the fractioning of functional protein between soluble and insoluble cell fractions in inclusion body-forming cells. Microb. Cell Fact. 5: 26.
13. Hardin, C., J. Edwards, A. Riell, D. Presutri, W. Miller, and D. Robertson. 2001. Time course assay of β-galactosidase, pp. 292-291. In: Cloning. Gene Expression. and Protein Purification: Experimental Procedures and Process Rationale. Oxford University Press.
14. Hoffmann, F., J. van den Heuvel, N. Zidek, and U. Rinas. 2004. Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and piiot plant scale. Enzyme Microb. Technol. 34: 235-241
15. Jevŝevar, S., V Gaberc-Porekar, I. Fonda, B. Podobnik, J. Grdadolnik, and V. Menart. 2005. Production of nonclassical inclusion bodies from which correctly folded protein can be extracted. Biotechnol. Prog. 21: 632-639.
16. Joo, J.-H. and J.-W. Yun. 2005. Structural and molecular characterization of extracellular polysaccharides produced by a new fungal strain, Trichoderma erinaceum DG-312. J. Microbiol. Biotechnol. 15: 1250-1257.
17. Lee, Y.-J. and K.-H. Jung. 2007. Modulation of the tendency towards inclusion body formation of recombinant protein by the addition of glucose in the araBAD promoter system of Escherichia coli. J. Microbiol. Biotechnol. 17: 1898-1903.
18. Kapust, R. B. and D. S. Waugh. 1999. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8: 1668-1674.
19. Koo, T. Y. and T. H. Park. 2007. Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate. J. Microbiol. Biotechnol. 17: 579-585.
20. Miller, J. M. 1973. Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
21. Mogk, A., M. P. Mayer, and E. Deuerling. 2002. Mechanisms of protein folding: Molecular chaperones and their application in biotechnology. Chembiochem 3: 807-814.
22. Schleif, R. 2000. Regulation of the L-arabinose operon of Escherichia coli. Trends Genet. 16: 559-565.
23. Sørensen, H. P. and K. K. Mortensen. 2005. Advanced genetic strategies fbr recombinant protein expression in Escherichia coli. J. Biotechnol. 115: 113-128.
24. Sørensen, H. P., H. U. Sperling-Petersen, and K. K. Mortensen. 2003. A favorable solubility partner for the recombinant expression of streptavidin. Protein Expr. Purif. 32: 252-259.
25. Strandberg, L. and S.-O. Enfors. 1991. Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli. Appl. Environ. Microbiol. 57: 1669-1674.
26. Tokatlidis, K., P. Dhurjati, J. Millet, P. Béguin, and J. P. Aubert. 1991. High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBS Lett. 282: 205-208.
27. van den Berg. B., R. J. Ellis, and C. M. Dobson. 1999. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18: 6927-6933.
28. Ventura, S. and A. Villaverde. 2006. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 24: 179-185.
29. Vera, A., N. González-Montalbán, A. Arís, and A. Villaverde. 2007. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol. Bioeng. 96: 1101-1106.
30. Worrall, D. M. and N. H. Goss. 1989. The formation of biologically active β-galactosidase inclusion bodies in Escherichia coli. Aust. J. Biotechnol. 3: 28-32.