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Received January 3, 2005
Accepted March 4, 2005
- This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Development of Novel Protein Refolding Using Simulated Moving Bed Chromatography
Department of Biological Engineering, Inha University, Incheon 402-751, Korea 1ERC for Advanced Bioseparation Technology, Inha University, Incheon 402-751, Korea
Korean Journal of Chemical Engineering, May 2005, 22(3), 425-432(8), 10.1007/BF02719422
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Abstract
In vitro protein refolding is still one of the baffles in both structural biology and development of new biopharmaceuticals, especially for large-scale production of valuable proteins that are overexpressed as inclusion bodies in Escherichia coli. A new continuous refolding method using four zone simulated moving bed process based on size exclusion mechanism was developed to overcome difficulties of inclusion body refolding. Protein refolding using size exclusion SMB enables us to obtain refolded protein continuously with high productivity, low consumption of refolding buffer, and high efficiency of size exclusion medium. Thermodynamics and kinetic parameters for SMB operation were estimated from the best-fit values by comparing the simulation and experimental chromatography results. The SMB operation condition was obtained from the triangle theory, and experimental results were in good agreement with the simulation results.
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References
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Batas B, Chaudhuri JB, J. Chromatogr. A, 864, 229 (1999)
Batas B, Jones HR, Chaudhuri JB, J. Chromatogr. A, 766, 109 (1997)
Batas B, Schiraldi C, Chaudhuri JB, J. Biotechnol., 68, 149 (1999)
Bollag DM, Rozycki MD, Edelstein SJ, Protein Methods, 2nd ed., Wiley, New York (1996)
Broughton DB, Chem. Eng. Prog., 64, 60 (1968)
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Daniel JS, Bachmann A, Hofrichter J, Hodgson KO, Doniach S, Kiefhaber T, J. Mol. Biol., 288, 489 (1999)
Elwell M, Schellman J, Biochimi. Biophysi. Act.(BBA)-Protein Structure, 359(1), 351 (1974)
Gao YG, Guan YX, Yao SJ, Cho MG, Korean J. Chem. Eng., 19(5), 871 (2002)
Geng X, Chang X, J. Chromatogr. A, 599, 185 (1992)
Gu Z, Su Z, Janson JC, J. Chromatogr. A, 918, 311 (2001)
Jacobson JM, Frenz JH, Horvath C, Ind. Eng. Chem. Res., 26, 43 (1987)
Jungbauer A, Kaar W, Schegl R, Curr. Opin. Biotechnol., 15, 487 (2004)
Jupke A, Epping A, Schnidt-Traub H, J. Chromatogr. A, 944, 93 (2002)
Kotlarski N, Oneill BK, Francis GL, Middelberg AP, AIChE J., 43(8), 2123 (1997)
Lanckriet H, Middelberg APJ, J. Chromatogr. A, 1022, 103 (2004)
Lee CT, Mackley MR, Stonestreet P, Middelberg APJ, Biotechnol. Lett., 23(22), 1899 (2001)
Ma Z, Wang NH, AIChE J., 43(10), 2488 (1997)
Mazzotti M, Storti G, Morbidelli M, J. Chromatogr. A, 769, 3 (1997)
Middelberg APJ, Biochem. Eng. J., 61(1), 41 (1996)
Pace CN, Methods Enzymol., 131, 266 (1986)
Pais LS, Loureiro JM, Rodrigues AE, Sep. Purif. Technol., 20, 67 (2000)
Rozema D, Gellman SH, J. Am. Chem. Soc., 117(8), 2373 (1995)
Saxena VP, Wetlaufer DB, Biochem, 9, 5015 (1970)
Shugar D, Biochim. Biophys. Acta, 8, 302 (1952)
Timasheff SN, Xie G, Biophys. Chem., 105, 421 (2003)
Wmer MH, Clore GM, Gronenborn AM, Kondoh A, Fisher RJ, Febs Lett., 345, 125 (1994)
Wildegger G, Kiefhaber T, J. Mol. Biol., 2792, 294 (1994)
Wu DJ, Xie Y, Ma Z, Wang NHL, Ind. Eng. Chem. Res., 37(10), 4023 (1998)
Yang YJ, Lee CH, Koo YM, Biotechnol. Bioprocess Eng., 9, 331 (2004)
Zhang Z, Mazzotti M, Morbidelli M, Korean J. Chem. Eng., 21(2), 454 (2004)