1. Scale-up of recombinant Opc protein production in Escherichia coli for a meningococcal vaccine
- Author
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José García Suárez, Raul Rafael Espinosa Perez, Alexis Musacchio Lasa, Evelin Caballero Menendez, Ricardo Silva Rodriguez, and Héctor Díaz Balaguer
- Subjects
Meningococcal Vaccines ,Bioengineering ,Meningitis, Meningococcal ,medicine.disease_cause ,Models, Biological ,Applied Microbiology and Biotechnology ,Inclusion bodies ,law.invention ,Microbiology ,law ,Escherichia coli ,medicine ,Humans ,Technology, Pharmaceutical ,biology ,Neisseria meningitidis ,General Medicine ,biology.organism_classification ,Enterobacteriaceae ,Recombinant Proteins ,stomatognathic diseases ,nervous system ,Recombinant DNA ,Neisseriaceae ,Bacterial outer membrane ,Bacteria ,Bacterial Outer Membrane Proteins ,Biotechnology - Abstract
Opc is an outer membrane protein from Neisseria meningitidis present in meningococcal vaccine preparations. The opc gene, codifying for this protein, was cloned in to Escherichia coli and the Opc protein was expressed under the control of a tryptophan promoter. The recombinant strain was grown in batch cultures. Opc was expressed as inclusion bodies at about 32% of the total cellular protein. We examined the scale-up culture conditions for the production of the recombinant Opc. The scale-up process was performed from 1.5 l to 50 l culture, using first, the constant power per unit of volume (P/V) as main scaling criteria, and then the oxygen mass transfer coefficient (K(L)a) scaling criteria to adjust the optimal aeration conditions. A final productivity of 52 mgl(-1)h(-1) was obtained at the 50l culture scale compared with the 49 mgl(-1)h(-1) productivity at 1.5l laboratory scale.
- Published
- 2006
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