Details
Originalsprache | Englisch |
---|---|
Seiten (von - bis) | 189-193 |
Seitenumfang | 5 |
Fachzeitschrift | IFAC Proceedings Volumes (IFAC-PapersOnline) |
Jahrgang | 37 |
Ausgabenummer | 3 |
Publikationsstatus | Veröffentlicht - 2004 |
Veranstaltung | 9th IFAC International Symposium on Computer Applications in Biotechnology, CAB 2004 - Nancy, Frankreich Dauer: 28 März 2004 → 31 März 2004 |
Abstract
For an industrial biotransformation process a simple mathematical model has been developed. Inuring the process indole and serine is converted to tryptophan using the enzyme tryptophan synthase, which is supplied in E. coli cells. The tryptophan production has been described by a first order kinetic with respect to serine and the relative cell concentration as well as zero order kinetics with respect to indole. The 10.000 L reactor, in which the production is performed, is described as an ideal stirred tank reactor. The activity of the cell suspension, i. e. the activity of the tryptophan synthase, which was considered in one of the model parameter could be determined from fluorescence measurements (fluorescence intensity at 350 nm excitation and 470 nm emission wavelength) using a linear regression model. The model prediction corresponds very well with off-line measurement.
ASJC Scopus Sachgebiete
- Ingenieurwesen (insg.)
- Steuerungs- und Systemtechnik
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in: IFAC Proceedings Volumes (IFAC-PapersOnline), Jahrgang 37, Nr. 3, 2004, S. 189-193.
Publikation: Beitrag in Fachzeitschrift › Konferenzaufsatz in Fachzeitschrift › Forschung › Peer-Review
}
TY - JOUR
T1 - Modelling of an industrial biotransformation process for tryptophan production
AU - Solle, Dörte
AU - Faurie, Robert
AU - Breccia, Javier
AU - Scheper, Thomas
AU - Hitzmann, Bernd
PY - 2004
Y1 - 2004
N2 - For an industrial biotransformation process a simple mathematical model has been developed. Inuring the process indole and serine is converted to tryptophan using the enzyme tryptophan synthase, which is supplied in E. coli cells. The tryptophan production has been described by a first order kinetic with respect to serine and the relative cell concentration as well as zero order kinetics with respect to indole. The 10.000 L reactor, in which the production is performed, is described as an ideal stirred tank reactor. The activity of the cell suspension, i. e. the activity of the tryptophan synthase, which was considered in one of the model parameter could be determined from fluorescence measurements (fluorescence intensity at 350 nm excitation and 470 nm emission wavelength) using a linear regression model. The model prediction corresponds very well with off-line measurement.
AB - For an industrial biotransformation process a simple mathematical model has been developed. Inuring the process indole and serine is converted to tryptophan using the enzyme tryptophan synthase, which is supplied in E. coli cells. The tryptophan production has been described by a first order kinetic with respect to serine and the relative cell concentration as well as zero order kinetics with respect to indole. The 10.000 L reactor, in which the production is performed, is described as an ideal stirred tank reactor. The activity of the cell suspension, i. e. the activity of the tryptophan synthase, which was considered in one of the model parameter could be determined from fluorescence measurements (fluorescence intensity at 350 nm excitation and 470 nm emission wavelength) using a linear regression model. The model prediction corresponds very well with off-line measurement.
KW - Automation
KW - Biotechnology
KW - Fluorescence
KW - Mathematical model
KW - Prediction
KW - Tryptophan production
UR - http://www.scopus.com/inward/record.url?scp=85083224598&partnerID=8YFLogxK
U2 - 10.1016/S1474-6670(17)32581-8
DO - 10.1016/S1474-6670(17)32581-8
M3 - Conference article
AN - SCOPUS:85083224598
VL - 37
SP - 189
EP - 193
JO - IFAC Proceedings Volumes (IFAC-PapersOnline)
JF - IFAC Proceedings Volumes (IFAC-PapersOnline)
SN - 1474-6670
IS - 3
T2 - 9th IFAC International Symposium on Computer Applications in Biotechnology, CAB 2004
Y2 - 28 March 2004 through 31 March 2004
ER -