Refolding techniques for recovering biologically active recombinant proteins from inclusion bodies

Biomolecules

Volumn 4, Issue 1, 2014, Pages 235-251

  Yamaguchi, Hiroshi ^a   Miyazaki, Masaya ^b,c  

^a TOKAI UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c KYUSHU UNIVERSITY   (Japan)

Author keywords

Chemical additive; Denatured protein; Inclusion body; Microfluidic chip; Protein refolding; Recombinant protein

Indexed keywords

AMINO ACID; ARGININE; CASEIN KINASE II; CYCLODEXTRIN; GAMMA INTERFERON; GLYCEROL; GLYCINAMIDE; GUANIDINE; INTERLEUKIN 21; MACROGOL; PROLINE; PROTEIN P53; RECOMBINANT PROTEIN; SUCROSE; TREHALOSE; UREA;

BIOLOGICAL ACTIVITY; DIALYSIS; DILUTION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE FUNCTION; GENE OVEREXPRESSION; LAMINAR FLOW; NONHUMAN; NUCLEAR MAGNETIC RESONANCE IMAGING; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MISFOLDING; PROTEIN REFOLDING; PROTEIN STRUCTURE; REVIEW; BIOCHEMISTRY; CELL INCLUSION; CHEMISTRY; EVALUATION STUDY; GENETICS; METABOLISM; PROCEDURES;

BIOCHEMISTRY; ESCHERICHIA COLI; INCLUSION BODIES; PROTEIN REFOLDING; RECOMBINANT PROTEINS;

EID: 84922789630     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom4010235     Document Type: Review

References (68)

1. Swartz, J.R. Advances in Escherichia coli production of therapeutic proteins. Curr. Opin. Biotechnol. 2001, 12, 195-201.
2. Clark, E.D.B. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 2001, 12, 202-207.
3. Baneyx. F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 1999, 10, 411-421.
4. Baneyx, F.; Mujacic, M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22, 1399-1408.
5. Prasad, S.; Khadatare, P.B.; Roy, I. Effect of chemical chaperones in improving the solubility of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol. 2011, 77, 4603-4609.
6. Li, M.; Su, Z.-G.; Janson, J.-C. In vitro protein refolding by chromatographic procedures. Protein Expr. Purif. 2004, 33, 1-10.
7. Sakono, M.; Kawashima, Y.; Ichinose, H.; Maruyama, T.; Kamiya, N.; Goto, M. Direct refolding of inclusion bodies using reversed micelles. Biotechnol. Prog. 2004, 20, 1783-1787.
8. Nara, T.Y.; Togashi, H.; Sekikawa, C.; Kawakami, M.; Yaginuma, N.; Sakaguchi, K.; Mizukami, F.; Tsunoda, T. Use of zeolite to refold a disulfide-bonded protein. Colloids Surf. B Biointerfaces. 2009, 68, 68-73.
9. Zhi, W.; Landry, S.J.; Gierasch, L.M.; Srere, P.A. Renaturation of citrate synthase: Influence of denaturant and folding assistants. Protein Sci. 1992, 1, 522-529.
10. Eiberle, M.K.; Jungbauer, A. Technical refolding of proteins: Do we have freedom to operate? Biotechnol. J. 2010, 5, 547-559.
11. Gautam, S.; Dubey, P.; Rather, G.M.; Gupta, M.N. Non-chromatographic strategies for protein refolding. Recent Pat. Biotechnol. 2012, 6, 57-68.
12. Machold, C.; Schlegl, R.; Buchinger, W.; Jungbauer, A. Matrix assisted refolding of proteins by ion exchange chromatography. J. Biotechnol. 2005, 117, 83-97.
13. Zhi, W.; Landry, S.J.; Gierasch L.M.; Srere, P.A. Renaturation of citrate synthase: Influence of denaturant and folding assistants. Protein Sci. 1992, 1, 522-529.
14. Reddy, K.R.C.; Lilie, H.; Rudolph, R.; Lange, C. L-Arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci. 2005, 14, 929-935.
15. Yamaguchi, H.; Miyazaki, M.; Briones-Nagata, M.P.; Maeda. H. Refolding of difficult-to-fold proteins by a gradual decrease of denaturant using microfluidic chips. J. Biochem. 2010, 147, 895-903.
16. Marston, F.A.O. The purification of eukaryotic polypeptides synthesized in Escherichia coli. Biochem. J. 1986, 240, 1-12.
17. Tsumoto, K.; Ejima, D.; Kumagai I.; Arakawa, T. Practical considerations in refolding proteins from inclusion bodies. Protein Expr. Purif. 2003, 28, 1-8.
18. Umetsu, M.; Tsumoto, K.; Hara, M.; Ashish, K.; Goda, S.; Adschiri, T.; Kumagai, I. How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment. J. Biol. Chem. 2003, 278, 8979-8987.
19. Ho, J.G.S.; Middelberg, A.P.J.; Ramage P.; Kocher, H.P. The likelihood of aggregation during protein renaturation can be assessed using the second virial coefficient. Protein Sci. 2003, 12, 708-716.
20. Liu, W.; Cellmer, T.; Keerl, D.; Prausnitz, J.M.; Blanch, H.W. Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements. Biotchnol. Bioeng. 2005, 90, 482-490.
21. Hevehan, D.L.; Clark, E.D.B. Oxidative renaturation of lysozyme at high concentrations. Biotechnol. Bioeng. 1997, 54, 221-230.
22. Orsini, G.; Goldberg, M.E. The renaturation of reduced chymotrypsinogen A in guanidine HCl. Refolding versus aggregation. J. Biol. Chem. 1978, 253, 3453-3458.
23. Yamaguchi, S.; Yamamoto, E.; Mannen, T.; Nagamune T. Protein refolding using chemical refolding additives. Biotechnol. J. 2013, 8, 17-31.
24. Kudou, M.; Yumioka, R.; Ejima, D.; Arakawa, T.; Tsumoto, K. A novel protein refolding system using lauroyl-L-glutamate as a solubilizing detergent and arginine as a folding assisting agent. Protein Expr. Purif. 2011, 75, 46-54.
25. Ohtake, S.; Kita, Y.; Arakawa, T. Interactions of formulation excipients with proteins in solution and in the dried state. Adv. Drug Deliv. Rev. 2011, 63, 1053-1073.
26. Lin, W.J.; Traugh, J.A. Renaturation of casein kinase II from recombinant subunits produced in Escherichia coli: Purification and characterization of the reconstituted holoenzyme. Protein Expr. Purif. 1993, 3, 256-264.
27. Arora, D.; Khanna, N. Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J. Biotechnol. 1996, 52, 127-133.
28. Bell, S.; Hansen, S.; Buchner, J. Refolding and structural characterization of the human p53 tumor suppressor protein. Biophys. Chem. 2002, 96, 243-257.
29. Asano, R.; Kudo, T.; Makabe, K.; Tsumoto, K.; Kumagai, I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichia coli. FEBS Lett. 2002, 528, 70-76.
30. Mande, S.C.; Sobhia, M.E. Structural characterization of protein-denaturant interactions: Crystal structures of hen egg-white lysozyme in complex with DMSO and guanidinium chloride. Protein Eng. 2000, 13, 133-141.
31. Ito, L.; Shiraki, K.; Matsuura, T.; Okumura, M.; Hasegawa, K.; Baba, S.; Yamaguchi, H.; Kumasaka, T. High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: Implication of suppression of protein aggregation by arginine. Protein. Eng. Des. Sel. 2011, 24, 269-274.
32. Matsuoka, T.; Hamada, H.; Matsumoto, K.; Shiraki, K. Indispensable structure of solution additives to prevent inactivation of lysozyme for heating and refolding. Biotechnol. Prog. 2009, 25, 1515-1524.
33. Hamada, H.; Shiraki, K. L-Argininamide improves the refolding more effectively than L-arginine. J. Biotechnol. 2007, 130, 153-160.
34. Ito, L.; Shiraki, K.; Makino, M.; Hasegawa, K.; Kumasaka, T. Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation. FEBS Lett. 2011, 585, 555-560.
35. Samuel, D.; Kumar, T.K.; Ganesh, G.; Jayaraman, G.; Yang, P.W.; Chang, M.M.; Trivedi, V.D.; Wang, S.L.; Hwang, K.C.; Chang, D.K.; Yu, C. Proline inhibits aggregation during protein refolding. Protein Sci. 2000, 9, 344-352.
36. Timasheff, S.N. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 2002, 41, 13473-13482.
37. Kohyama, K.; Matsumoto, T.; Imoto, T. Refolding of an unstable lysozyme by gradient removal of a solubilizer and gradient addition of a stabilizer. J. Biochem. 2010, 147, 427-431.
38. Nian, R.; Kim, D.S.; Tan, L.; Kim, C.W.; Choe, W.S. Synergistic coordination of polyethylene glycol with ClpB/DnaKJE bichaperone for refolding of heat-denatured malate dehydrogenase. Biotechnol. Prog. 2009, 25, 1078-1085.
39. Webb, S.D.; Cleland, J.L.; Carpenter, J.F.; Randolph, T.W. A new mechanism for decreasing aggregation of recombinant human interferon-gamma by a surfactant: Slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20. J. Pharm. Sci. 2002, 91, 543-558.
40. Akbari, N.; Khajeh, K.; Ghaemi, N.; Salemi, Z. Efficient refolding of recombinant lipase from Escherichia coli inclusion bodies by response surface methodology. Protein Expr. Purif. 2010, 70, 254-259.
41. Paul, S.; Punam, S.; Chaudhuri, T.K. Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase. FEBS J. 2007, 274, 6000-6010.
42. Wang, F.; Liu, Y.; Li, J.; Ma, G.; Su, Z. On-column refolding of consensus interferon at high concentration with guanidine-hydrochloride and polyethylene glycol gradients. J. Chromatogr. A. 2006, 1115, 72-80.
43. Hart; R.A.; Lester, P.M.; Reifsnyder, D.H.; Ogez, J.R.; Builder, S.E. Large scale, in situ isolation of periplasmic IGF-I from E. coli. Bio/Technol. 1994, 12, 1113-1117.
44. Bajorunaite, E.; Cirkovas, A.; Radzevicius, K.; Larsen, K.L.; Sereikaite, J.; Bumelis, V.A. Anti-aggregatory effect of cyclodextrins in the refolding process of recombinant growth hormones from Escherichia coli inclusion bodies. Int. J. Biol. Macromol. 2009, 44, 428-434.
45. Sharma, L.; Sharma, A. Influence of cyclodextrin ring substituents on folding-related aggregation of bovine carbonic anhydrase. Eur. J. Biochem. 2001, 268, 2456-2463.
46. Vandevenne, M.; Gaspard, G.; Belgsir, E.M.; Ramnath, M.; Cenatiempo, Y.; Marechal, D.; Dumoulin, M.; Frere, J.M.; Matagne, A.; Galleni, M.; Filee, P. Effects of monopropanediamino-ß-cyclodextrin on the denaturation process of the hybrid protein BlaPChBD. Biochim. Biophys. Acta. 2011, 1814, 1146-1153.
47. Daugherty, D.L.; Rozema, D.; Hanson, P.E.; Gellman, S.H. Artificial chaperone-assisted refolding of citrate synthase. J. Biol. Chem.1998, 273, 33961-33971.
48. Rozema, D.; Gellman, S.H. Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 1996, 271, 3478-3487.
49. Machida, S.; Ogawa, S.; Xiaohua, S.; Takaha, T.; Fujii, K.; Hayashi, K. Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett. 2000, 486, 131-135.
50. Haeberle, S.; Zengerle, R.K. Microfluidic platforms for lab-on-a-chip applications. Lab Chip 2007, 7, 1094-1110.
51. Ohno, K.; Tachikawa, K.; Manz, A. Microfluidics: Applications for analytical purposes in chemistry and biochemistry. Electrophoresis 2008, 29, 4443-4453.
52. Asanomi, Y.; Yamaguchi, H.; Miyazaki, M.; Maeda, H. Enzyme-immobilized microfluidic process reactors. Molecules 2011, 16, 6041-6059.
53. Yamaguchi, H.; Maeki, M.; Yamashita, K.; Nakamura, H.; Miyazaki, M.; Maeda, H. Controlling one protein crystal growth by droplet-based microfluidic system. J. Biochem. 2013, 153, 339-346.
54. Lapidus, L.J.; Yao, S.; Mcgarrity, K.S.; Hertzog, D.E.; Tubman, E.; Bakajin, O. Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer. Biophys. J. 2007, 93, 218-224.
55. Kane, A.S.; Hoffmann, A.; Baumgärtel, P.; Seckler, R.; Reichardt, G.; Horsley, D.A.; Schuler, B.; Bakajin, O. Microfluidic mixers for the investigation of rapid protein folding kinetics using synchrotron radiation circular dichroism spectroscopy. Anal. Chem. 2008, 80, 9534-9541.
56. Hertzog, D.E.; Michalet, X.; Jäger, M.; Kong, X.; Santiago, J.G.; Weiss, S.; Bakajin, O. Femtomole mixer for microsecond kinetic studies of protein folding. Anal. Chem. 2004, 76, 7169-7178.
57. Kerby, M.B.; Lee, J.; Ziperstein, J.; Tripathi, A. Kinetic measurements of protein conformation in a microchip. Biotechnol. Prog. 2006, 22, 1416-1425.
58. Yamamoto, E.; Yamaguchi, S.; Sasaki, N.; Kim, H.-B.; Kitamori, T.; Nagamune, T. Artificial chaperone-assisted refolding in a microchannel. Bioprocess Biosyst. Eng. 2010, 33, 171-177.
59. Karnik, R.; Gu, F.; Basto, P.; Cannizzaro, C.; Dean, L.; Kyei-Manu, W.; Langer, R.; Farokhzad, O.C. Microfluidic platform for controlled synthesis of polymeric nanoparticles. Nano Lett. 2008, 8, 2906-2912.
60. Hong, S.; Tsou, P.H.; Chou, C.K.; Yamaguchi, H.; Su, C.B.; Hung, M.C.; Kameoka, J. Microfluidic three-dimensional hydrodynamic flow focusing for the rapid protein concentration analysis. Biomicrofluidics 2012, 6, 24132.
61. Dayel, M.J.; Hom, E.F.; Verkman, A.S. Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys. J. 1999, 76, 2843-2851.
62. Gosting, L.J.; Akeley, D.F. A study of the diffusion of urea in water at 25° with the Gouy interference method. J. Am. Chem. Soc. 1952, 74, 2058-2060.
63. Jahn, A.; Vreeland, W.N.; deVoe, D.L.; Locascio, L.E.; Gaitan, M. Microfluidic directed formation of liposomes of controlled size. Langmuir 2007, 23, 6289-6293.
64. Jin, L.; Pluskey, S.; Petrella, E.C.; Cantin, S.M.; Gorga, J.C.; Rynkiewicz, M.J.; Pandey, P.; Strickler, J.E.; Babine, R.E.; Weaver, D.T.; Seidl, K.J. The three-dimensional structure of the ZAP-70 kinase domain in complex with staurosporine. J. Biol. Chem. 2004, 279, 42818-42825.
65. Visco, C.; Magistrelli, G.; Bosotti, R.; Perego, R.; Rusconi, L.; Toma, S.; Zamai, M.; Acuto O.; Isacchi, A. Activation of Zap-70 tyrosine kinase due to a structural rearrangement induced by tyrosine phosphorylation and/or ITAM binding. Biochemistry 2000, 39, 2784-2791.
66. Swietnicki, W. Folding aggregated proteins into functionally active forms. Curr. Opin. Biotechnol. 2006, 17, 367-372.
67. Ordidge, G.C.; Mannall, G.; Liddell, J.; Dalby, P.A.; Micheletti, M. A generic hierarchical screening method for the analysis of microscale refolds using an automated robotic platform. Biotechnol. Prog. 2012, 28, 435-444.
68. Nian, R.; Kim, D.S.; Tan, L.; Kim, C.W.; Choe, W.S. Synergistic coordination of polyethylene glycol with ClpB/DnaKJE bichaperone for refolding of heat-denatured malate dehydrogenase. Biotechnol. Prog. 2009, 25, 1078-1085.