Source:http://linkedlifedata.com/resource/pubmed/id/12242631
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2002-9-20
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pubmed:abstractText |
A simple structured model is proposed for simulating batch cultivation data on growth, substrate utilization, and heterologous enzyme production of recombinant Saccharomyces cerevisiae YPB-G. The enzyme is a fusion protein displaying alpha-amylase and glucoamylase activities. Cell growth is modulated mainly by intracellular substrate and ethanol concentrations. Intracellular substrate concentration is evaluated by means of the extracellular substrate and biomass concentrations. Extracellular alpha-amylase and glucoamylase activities are taken to depend on biomass concentration. The nine parameters of the proposed model are determined using nonlinear estimation techniques, and the model is validated against experiments not used in parameter determination. The model developed simulates glucose consumption, cell mass, alpha-amylase and glucoamylase production in a batch system. Simulation and experimental results are found to be in good agreement.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1367-5435
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
111-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12242631-Biomass,
pubmed-meshheading:12242631-Culture Media,
pubmed-meshheading:12242631-Glucan 1,4-alpha-Glucosidase,
pubmed-meshheading:12242631-Models, Biological,
pubmed-meshheading:12242631-Recombinant Proteins,
pubmed-meshheading:12242631-Saccharomyces cerevisiae,
pubmed-meshheading:12242631-Time Factors,
pubmed-meshheading:12242631-alpha-Amylases
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pubmed:year |
2002
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pubmed:articleTitle |
A simple structured model for biomass and extracellular enzyme production with recombinant Saccharomyces cerevisiae YPB-G.
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pubmed:affiliation |
Department of Chemical Engineering, Bogaziçi University, 80815 Bebek, Istanbul, Turkey.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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