Source:http://linkedlifedata.com/resource/pubmed/id/15257442
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2004-8-9
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pubmed:abstractText |
This paper provides an approach for optimizing the cell density (Xc) and dilution rate (D) in a chemostat for a Pichia pastoris continuous fermentation for the extracellular production of a recombinant protein, interferon tau (INF-tau). The objective was to maximize the volumetric productivity (Q, mg INF-tau l(-1) h(-1)), which was accomplished using response surface methodology (RSM) to model the response of Q as a function of Xc and D within the ranges 150< or = Xc < or =450 g cells (wet weight) l(-1) and 0.1 microm< or = D< or =0.9 microm (microm=0.0678 h(-1), the maximum specific growth rate obtained from a fed-batch phase controlled with a methanol sensor). The methanol and medium feed rates that resulted in the desired Xc and D were determined based on the mass balance. From the RSM model, the optimal Xc and D were 328.9 g l(-1) and 0.0333 h(-1) for a maximum Q of 2.73 mg l(-1) h(-1). The model of specific production rate (rho, mg INF-tau g(-1) cells h(-1)) was also established and showed the optimal Xc 287.7 g l(-1) and D=0.0361 h(-1) for the maximum rho (predicted to be 8.92 x 10(-3) mg(-1) g(-1) h(-1)). The methanol specific consumption rate (nu, g methanol g(-1) cells h(-1)) was calculated and shown to be independent of the cell density. The relationship between nu and mu (specific growth rate) was the same as that discovered from fed-batch fermentations of the same strain. The approach developed in this study is expected to be applicable to the optimization of continuous fermentations by other microorganisms.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Methanol,
http://linkedlifedata.com/resource/pubmed/chemical/Pregnancy Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/trophoblastin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1367-5435
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
330-4
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pubmed:meshHeading |
pubmed-meshheading:15257442-Biomass,
pubmed-meshheading:15257442-Bioreactors,
pubmed-meshheading:15257442-Biotechnology,
pubmed-meshheading:15257442-Culture Media,
pubmed-meshheading:15257442-Feedback,
pubmed-meshheading:15257442-Fermentation,
pubmed-meshheading:15257442-Industrial Microbiology,
pubmed-meshheading:15257442-Interferon Type I,
pubmed-meshheading:15257442-Mathematics,
pubmed-meshheading:15257442-Methanol,
pubmed-meshheading:15257442-Pichia,
pubmed-meshheading:15257442-Pregnancy Proteins,
pubmed-meshheading:15257442-Recombinant Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
Optimization of cell density and dilution rate in Pichia pastoris continuous fermentations for production of recombinant proteins.
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pubmed:affiliation |
Biological Process Development Facility, Department of Chemical Engineering, University of Nebraska-Lincoln, 207 Othmer Hall, Lincoln, NE 68588-0643, USA.
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pubmed:publicationType |
Journal Article
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