Refolding of proteins in a CSTR

Chemical Engineering Science

Volumn 60, Issue 21, 2005, Pages 5770-5780

  Schlegl, Robert ^a   Tscheliessnig, Anne ^b   Necina, Roman ^a   Wandl, Robert ^a   Jungbauer, Alois ^b  

^a BOEHRINGER INGELHEIM RCV GMBH AND CO KG   (Austria)

^b UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

Author keywords

Continuous refolding; CSTR; Diafiltration; Renaturation

Indexed keywords

DIFFERENTIAL EQUATIONS; REACTION KINETICS; RECYCLING; SIMULATED ANNEALING;

BATCH REFOLDING PROCESS; CONTINUOUS STIRRED TANK REACTOR (CSTR); DENATURING AGENTS; STIRRED TANK REACTORS;

PROTEINS;

PROTEIN;

EID: 22244443809     PISSN: 00092509     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ces.2005.04.086     Document Type: Article

References (20)

1. M. Arai, K. Ito, T. Inobe, M. Nakao, K. Maki, K. Kamagata, H. Kihara, Y. Amemiya, and K. Kuwajima Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering Journal of Molecular Biology 321 2002 121 132
2. T. Arakawa, and K. Tsumoto The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation Biochemical and Biophysical Research Communications 304 2003 148 152
3. M.A. Buswell, and A.P.J. Middelberg Critical analysis of lysozyme refolding kinetic Biotechnology Progress 18 2002 470 475
4. M.A. Buswell, M. Ebtinger, A.A. Vertés, and A.P.J. Middelberg Effect of operating variables on the yield of recombinant trypsinogen for a pulse-fed dilution-refolding reactor Biotechnology and Bioengineering 77 2002 435 444
5. E.D. Clark, and L.D. Hevehan Oxidative renaturation of lysozyme at high concentrations Biotechnology and Bioengineering 54 1997 221 230
6. H. Edelhoch Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6 1967 1948 1954
7. J.J. Ewbank, and T.E. Creighton Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin Biochemistry 32 1993 3694 3707
8. B. Fischer, B. Perry, I. Summer, and P. Goodenough A novel sequential procedure to enhance the renaturation of recombinant protein from E.coli inclusion bodies Protein Engineering 5 1992 593 596
9. M. Goldberg, R. Rudolph, and R. Jaenicke A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme Biochemistry 30 1991 2790 2797
10. S. Katoh, and Y. Katoh Continuous refolding of lysozyme with fed-batch addition of denatured protein solution Process Biochemistry 35 2000 1119 1124
11. T. Kiefhaber, R. Rudolph, H. Kohler, and J. Buchner Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation Bio-Technology 9 1991 825 829
12. Levenspiel, O., 1999. Chemical Reaction Engineering, third ed. Wiley, NY, pp. 175-180.
13. A.P.J. Middelberg The influence of protein refolding strategy on cost for competing reactions Chemical Engineering Journal 61 1996 41 52
14. E.A. Permyakov, and L.J. Berliner Alpha-lactalbumin: structure and function FEBS Letters 473 2000 269 274
15. Rutherford, A., 1999. Elementary Chemical Reactor Analysis. Dover Publications Inc., NY, p. 161.
16. R. Schlegl, G. Iberer, C. Machold, R. Necina, and A. Jungbauer Continuous matrix-assisted refolding of proteins Journal of Chromatography A 1009 2003 119 132
17. M. Terashima, K. Suzuki, and S. Katoh Effective refolding of fully reduced lysozyme with a flow-type reactor Process Biochemistry 31 1996 341 345
18. D.B. Wetlaufer, and Y. Xie Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II Protein Science 4 1995 1535 1543
19. L.C. Wu, B.A. Schulman, Z.Y. Peng, and P.S. Kim Disulfide determinants of calcium-induced packing in alpha-lactalbumin Biochemistry 35 1996 859 863
20. G. Zettlmeissl, R. Rudolph, and R. Jaenicke Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation Biochemistry 18 1979 5567 5571