Recombinant Protein Production with Prokaryotic and Eukaryotic Cells. A Comparative View on Host Physiology

1. Front Matter

   Pages i-x

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2. Cell-free translation systems

   1. Protein Synthesis and Co-Translational Folding in Cell-Free Translation Systems

      • Alexander S. Spirin

      Pages 1-15

3. Metabolic burden and stress response

   1. The Cellular Response to Unfolded Proteins in the Endoplasmic Reticulum

      • Randal J. Kaufman, Donalyn Scheuner, Witoon Tirasophon, Chuan Yin-Liu, Benbo Song, Kuei C. Lee et al.

      Pages 17-27

   2. The Effects of Recombinant Protein Expression on the Growth and Metabolism of Mammalian Cells

      • C. A. Yallop, I. Svendsen

      Pages 29-42

   3. Mapping Stresses in Escherichia Coli to Improve Yield

      • Matthew P. DeLisa, Ryan T. Gill, William E. Bentley

      Pages 43-54

   4. Cellular Responses to Strong Overexpression of Recombinant Genes in Escherichia Coli

      • Hong Ying Lin, Renate Hanschke, Silke Nicklisch, Stephan Riemschneider, Sylke Meyer, Antje Gupta et al.

      Pages 55-73

   5. From Vitreoscilla Hemoglobin (VHb) to a Novel Class of Growth Stimulating Hemoglobin Proteins

      • Pauli T. Kallio, Alexander D. Frey, James E. Bailey

      Pages 75-87

4. Genetic stability and gene copy number effects

   1. Protein Mass Production in Hybridomas and Recombinant CHO Cells

      • R. Kunert, K. Strutzenberger, F. Steindl, A. Zudjelovic, N. Borth, H. Katinger

      Pages 89-97

   2. Inducible Gene Copy Number Amplification for the Production of Heterologous Proteins in Kluyveromyces lactis

      • Michele M. Bianchi

      Pages 99-110

   3. Antibiotic-Free Plasmid Selection and Maintenance in Bacteria

      • Julian A. J. Hanak, Rocky M. Cranenburgh

      Pages 111-124

   4. Modelling of Segregational Plasmid Instability of Recombinant Strain Suspension of Escherichia coli

      • Joseph Boudrant, Baolinh Le, Frantz Fournier, Christian Fonteix

      Pages 125-139

5. Transcription, translation, and product formation in E. coli

   1. Production of Optically Pure Aryl Epoxides by Recombinant E. coli Carrying Styrene Monooxygenase

      • A. Colmegna, E. Galli, G. Sello, G. Bestetti

      Pages 141-149

   2. Translational Problems Associated with the Rare Arginine Codon CGG in Escherichia Coli

      • Dean E. McNulty, Michael J. Huddleston, Brett Claffee, Susan Green, Ganesh Sathe, Robert Reeves et al.

      Pages 151-158

   3. Optimisation of the Solubility of the Recombinant Itk Kinase Domain in Escherichia Coli

      • Nina Q. Meinander, Marie Jeppsson, Morten Sögaard

      Pages 159-170

   4. Bacterial Senescence and the Oxidation Paradox

      • Thomas Nyström, Manuel Ballesteros, Åsa Fredriksson

      Pages 171-178

   5. Metabolic Approaches for the Optimisation of Recombinant Fermentation Processes

      • Gerald Striedner, Monika Cserjan-Puschmann, Reingard Grabherr, Franz Clementschitsch, Erik Nilsson, Karl Bayer

      Pages 179-188

   6. Control and Optimisation of Cellular Bottlenecks in Recombinant Protein Production

      • Anna Maria Sanden, Gen Larsson

      Pages 189-194

   7. Expression and Fermentation Strategies for Recombinant Protein Production in Escherichia Coli

      • P. Neubauer, J. Winter

      Pages 195-258

6. Transcription, translation, and product formation in microbial systems other than E. coli

   1. Overexpression of a Rhizopus Oryzae Lipase in Pichia Pastoris Strains Containing Multiple Copies of the Target Gene

      • A. Serrano, G. Lin Cereghino, P. Ferrer, J. M. Cregg, F. Valero

      Pages 259-267

   2. Development of a Heterologous Gene Expression System for Use in Lactococcus Lactis

      • L. Bredmose, S. M. Madsen, A. Vrang, P. Ravn, M. G. Johnsen, J. Glenting et al.

      Pages 269-275

More then 20 years have passed now since the first recombinant protein producing microorganisms have been developed. In the meanwhile, numerous proteins have been produced in bacteria, yeasts and filamentous fungi, as weIl as higher eukaryotic cells, and even entire plants and animals. Many recombinant proteins are on the market today, and some of them reached substantial market volumes. On the first sight one would expect the technology - including the physiology of the host strains - to be optimised in detail after a 20 year's period of development. However, several constraints have limited the incentive for optimisation, especially in the pharmaceutical industry like the urge to proceed quickly or the requirement to define the production parameters for registration early in the development phase. The additional expenses for registration of a new production strain often prohibits a change to an optimised strain. A continuous optimisation of the entire production process is not feasible for the same reasons.

• Bur
• Codons
• DNA
• Fermentation
• Mammalia
• Metabolism
• Oxidation
• Translation
• biotechnology
• development
• gene expression
• genes
• microorganism
• proteins
• transcription
• biochemical engineering

• Genethon III, Evry-Cedex, France

  O.-W. Merten

• Institute for Applied Microbiology, University of Agricultural Sciences, Wien, Austria

  D. Mattanovich

• Institute of Biotechnology, Technical University of Berlin, Berlin, Germany

  C. Lang

• The Swedish Centre on Bioprocess Technology, KTH, Stockholm, Sweden

  G. Larsson

• Institute of Biotechnology, M. Luther University of Halle-Wittenberg, Halle, Germany

  P. Neubauer

• Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy

  D. Porro

• E.C. Slater Institute, University of Amsterdam, The Netherlands

  P. Postma

• Swammerdam Institute of Life Sciences, University of Amsterdam, The Netherlands

  J. Teixeira Mattos

• School of Biosciences, University of Birmingham, UK

  J. A. Cole

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