Towards molecular farming in the future: pichia pastoris-based production of single-chain antibody fragments.
This review article focuses on the use of the methylotrophic yeast Pichia pastoris as a recombinant protein-expression system. P. pastoris is a useful system for the expression of milligram-to-gram quantities of a protein, which can be scaled up to fermentation to meet greater demands. Compared with mammalian cells, Pichia do not require a complex growth medium or culture conditions, they are as easy to manipulate genetically as Escherichia coli and have a eukaryotic protein-synthesis pathway. They seem suited to laboratory-scale production of recombinant proteins for in-house use or, in some cases, molecular farming of recombinant products. This review article focuses on the use of P. pastoris, describes a fermentation production run of a single-chain antibody fragment and includes a discussion of fermentation as a production strategy.
Fischer
R
R
Fraunhofer Department for Molecular Biotechnology, IUCT, Grafschaft, Auf dem Aberg 1, D-57392 Schmallenberg, Germany.
Drossard
J
J
Emans
N
N
Commandeur
U
U
Hellwig
S
S
D003001:Cloning, Molecular; D005285:Fermentation; D005544:Forecasting; D007128:Immunoglobulin Fragments / Q000235:genetics* / Q000378:metabolism; D010843:Pichia / Q000235:genetics* / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods* / Q000639:trends; D011994:Recombinant Proteins / Q000235:genetics* / Q000378:metabolism*; D012641:Selection, Genetic; D014170:Transformation, Genetic
D007128:Immunoglobulin Fragments; D011994:Recombinant Proteins; C055966:immunoglobulin Fv