Modeling of protein refolding from inclusion bodies

Acta Biochimica et Biophysica Sinica

Volumn 41, Issue 12, 2009, Pages 1044-1052

  Zhang, Ting ^a   Xu, Xiaojing ^b   Shen, Liang ^c   Feng, Yanye ^a   Yang, Zhong ^a   Shen, Yaling ^a   Wang, Jufang ^d   Jin, Weirong ^b   Wang, Xiaoning ^a,d  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b NATIONAL ENGINEERING CENTER FOR BIOCHIP AT SHANGHAI   (China)

^c SHANDONG UNIVERSITY OF FINANCE AND ECONOMICS   (China)

^d SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Escherichia coli; Inclusion body; Protein refolding; Statistical modeling

Indexed keywords

BUFFER; ESCHERICHIA COLI PROTEIN;

ARTICLE; BIOLOGICAL MODEL; CELL INCLUSION; CHEMISTRY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; ISOELECTRIC POINT; METABOLISM; MOLECULAR WEIGHT; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUBILITY;

BUFFERS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION; INCLUSION BODIES; ISOELECTRIC POINT; MODELS, BIOLOGICAL; MOLECULAR WEIGHT; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUBILITY;

ESCHERICHIA COLI;

EID: 71949106957     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmp098     Document Type: Article

References (33)

1. Makrides SC. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 1996, 60: 512-538.
2. Baneyx F and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 2004, 22: 1399-1408.
3. Baneyx F. Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol 1999, 10: 411-421.
4. Marston FA. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem J 1986, 240: 1-12.
5. Singh SM and Panda AK. Solubilization and refolding of bacterial inclusion body proteins. J Biosci Bioeng 2005, 99: 303-310.
6. Rudolph R and Lilie H. In vitro folding of inclusion body proteins. FASEB J 1996, 10: 49-56.
7. Villaverde A and Carrio MM. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 2003, 25: 1385-1395.
8. Datar RV, Cartwridht T and Rosen CG. Process economic of animal cell and bacterial fermentations: A case study analysis of tissue plasminogen activator. Biotechnology 1993, 11: 349-357.
9. Strandberg L and Enfors SO. Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli. Appl Environ Microbiol 1991, 57: 1669-1674.
10. Hoffmann F and Rinas U. Roles of heat-shock chaperones in the production of recombinant proteins in Escherichia coli. Aust J Biochem Eng Biotechnol 2004, 89: 143-161.
11. Ventura S and Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol 2006, 4: 179-185.
12. Markus K, Markus F, Sandra B and Pleiss J. How to find soluble proteins: A comprehensive analysis of a/b hydrolases for recombinant expression in E. coli. BMS Genomics 2005, 6: 49-58.
13. Zettimeissl C, Rudolph R and Jaenicke R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. Physical properties and kinetics of aggregation. Biochemistry 1979, 18: 5567-5571.
14. Willkinson DL and Harrison RG. Predicting the solubility of recombinant proteins in Escherichia coli. Biotechnology 1991, 9: 443-448.
15. Tsumoto K, Umetsu M, Kumagai I, Ejima D, Philo JS and Arakawa T. Role of arginine in protein refolding, solubilization, and purification. Biotechnol Prog 2004, 20: 1301-1308.
16. Katoh S, Sezai Y, Yamaguchi T, Katoh Y, Yagi H and Nohara D. Refolding of enzymes in a fed-batch operation. Process Biochem 1999, 35: 297-300.
17. Jungbauer A and Kaar W. Current status of technical protein refolding. J Biotechnol 2007, 128: 587-596.
18. Vallejo LF and Rinas U. Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins. Microb Cell Fact 2004, 3: 1-12.
19. Vallejo LF and Rinas U. Optimized procedure for denaturation of recombinant human bone morphogenetic protein-2 at high protein concentration. Biotechnol Bioeng 2004, 85: 601-609.
20. Jungbauer A, Kaar W and Schlegl R. Folding and refolding of proteins in chromatographic beds. Curr Opin Biotechnol 2004, 15: 487-494.
21. Lefebvre BG, Gage MJ and Robinson AS. Maximizing recovery of native protein from aggregates by optimizing pressure treatment. Biotechnol Prog 2004, 20: 623-629.
22. Ho JG and Middelberg AP. Estimating the potential refolding yield of recombinant proteins expressed as inclusion bodies. Biotechnol Bioeng 2004, 87: 584-592.
23. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72: 248-254.
24. Trivedi VD, Raman B, Rao CM and Ramakrishna T. Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteins. FEBS Lett 1997, 418: 363-366.
25. London J, Skrzynia C and Goldberg ME. Denaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Eur J Biochem 1974, 47: 407-415.
26. Das U, Hariprasad G, Ethayathulla AS, Manral P, Das TK, Pasha S and Mann A, et al. Inhibition of protein aggregation: supramolecular assemblies of arginine hold the key. PLoS ONE 2007, 2: e1176.
27. Cleland JL and Wang DI. Co-solvent assisted protein refolding. Biotechnology 1990, 8: 1274-1278.
28. Zerella R, Chen PY, Evans PA and Raine A. Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding. Protein Sci 2000, 9: 2142-2150.
29. Wentzel A, Christmann A, Kratzner R and Kolmar H. Sequence requirements of the GPNG b-turn of the Ecballium elaterium trypsin inhibitor II explored by combinatorial library screening. J Biol Chem 1999, 274: 1037-1043.
30. Ami D, Bonecchi L, Cal?̀ S, Orsini G, Tonon G and Doglia SM. FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim Biophys Acta 2003, 1624: 6-10.
31. Carrió M, González-Montalbán N, Vera A, Villaverde A and Ventura S. Amyloid-like properties of bacterial inclusion bodies. J Mol Biol 2005, 347: 1025-1037.
32. Ami D, Natalello A, Gatti-Lafranconi P, Lotti M and Doglia SM. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett 2005, 579: 3433-3436.
33. Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci 1999, 24: 329-332.