Fast quantification of recombinant protein inclusion bodies within intact cells by FT-IR spectroscopy

Biotechnology Progress

Volumn 23, Issue 3, 2007, Pages 762-766

  Gross Selbeck, Sven ^a   Margreiter, Gerd ^a   Obinger, Christian ^a   Bayer, Karl ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ELECTROPHORESIS; ESCHERICHIA COLI; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MATHEMATICAL MODELS; SILICON;

INCLUSION BODY; MULTIVARIATE CALIBRATION; MULTIVARIATE MODEL;

PROTEINS;

RECOMBINANT PROTEIN;

ARTICLE; CELL INCLUSION; CYTOLOGY; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; METABOLISM; METHODOLOGY; REPRODUCIBILITY;

ESCHERICHIA COLI; INCLUSION BODIES; RECOMBINANT PROTEINS; REPRODUCIBILITY OF RESULTS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 34250351307     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp070022q     Document Type: Article

References (16)

1. Misawa, S.; Kumagai, I. Refolding of therapeutic proteins produced in Escherichia coli as inclusion bodies. Biopolymers 1999, 51, 297-307.
2. Khan, R. H.; Rao, K. B.; Eshwari, A. N.; Totey, S. M.; Panda, A. K. Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli. Biotechnol. Prog. 1998, 14, 722-728.
3. Singh, S. M.; Panda, A. K. Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 2005, 99, 303-310.
4. Fahnert, B.; Lilie, H.; Neubauer, P. Inclusion bodies: formation and utilisation. Adv. Biochem. Eng. Biotechnol. 2004, 89, 93-142.
5. Hinsmann, P.; Frank, J.; Svasek, P.; Harasek, M.; Lendl, B Design, simulation and application of a new micromixing device for time resolved infrared spectroscopy of chemical reactions in solution. Lab Chip 2001, 1, 16-21.
6. Ngo-Thi, N. A.; Kirschner, C.; Naumann. D. Characterization and identification of microorganisms by FIF-1R microspectrometry. J. Mol. Struct. 2003, 661, 371-380.
7. Helm, D.; Labischinski, H.; Schallehn, G.; Naumann, D. Classification and identification of bacteria by Fourier-Transform Infrared-Spectroscopy. J. Gen. Microbiol. 1991, 137, 69-79.
8. Naumann, D. Infrared spectroscopy in microbiology. In Encyclopedia of Analytical Chemistry; Wiley: New York, 2000.
9. Dominguez-Vidal, A.; Saenz-Navajas, M. P.; Ayora-Canada, M. J.; Lendl, B. Detection of albumin unfolding preceding proteolysis using fourier transform infrared spectroscopy and chemometric data analysis. Anal. Chem. 2006, 78, 3257-3264.
10. Hering, J. A.; Innocent, P. R.; Haris, P. I. Automatic amide I frequency selection for rapid quantification of protein secondary structure from Fourier transform infrared spectra of proteins. Proteomics 2002, 2, 839-849.
11. Esbensen, K. Multivariate Data Analysis-In Practice, 5th ed.; Camo Process AS: Oslo, 2001.
12. Clementschitsch, F.; Jurgen, K.; Florentina, P.; Karl, B. Sensor combination and chemometric modelling for improved process monitoring in recombinant E. coli fed-batch cultivations. J. Biotechnol. 2005, 120, 183-196.
13. Reischer, H.; Schotola, I.; Striedner, G.; Potschacher, F.; Bayer, K. Evaluation of the GFP signal and its aptitude for novel on-line monitoring strategies of recombinant fermentation processes. J. Biotechnol. 2004, 108, 115-125.
14. Kromidas, S. Validierung in der Anatytik; Wiley-VCH: Weinheim, 1999.
15. Ami, D.; Natalello, A.; Taylor, G.; Tonon, G.; Maria, Doglia, S. Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy. Biochim. Biophys. Acta 2006, 1764, 793-799.
16. Carrio, M.; Gonzalez-Montalban, N.; Vera, A.; Villaverde, A.; Ventura, S. Amyloid-like properties of bacterial inclusion bodies. J. Mol. Biol. 2005, 347, 1025-1037.