Details
| Original language | English |
|---|---|
| Pages (from-to) | B13-B19 |
| Journal | The Chemical Engineering Journal |
| Volume | 52 |
| Issue number | 1 |
| Publication status | Published - Aug 1993 |
Abstract
The enzymatic hydrolysis of potato pulp by a cell-free culture filtrate of Trichoderma reesei Rut C30 was studied. On the basis of the experimental data a dynamic unstructured model using Michaelis-Menten kinetics was developed. This mathematical model describes the enzymatic hydrolysis in terms of the adsorption and desorption of enzymes on the solid substrate and with regard to competitive and uncompetitive inhibition. The model equations consist of a non-linear system of ordinary differential and algebraic equations. Parameter identification was done by dividing the model into submodels and fitting these to experimental data. The simulation results with the model correspond well with the experimental data. Thus the good agreement between simulated and measured process variables indicates that the model is suitable for description of the enzymatic hydrolysis. Computations for different operational conditions show the range of validity and performance of the model. Possibilities for improvements in yield and productivity could be deduced by model computations.
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In: The Chemical Engineering Journal, Vol. 52, No. 1, 08.1993, p. B13-B19.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Modelling and simulation of the enzymatic hydrolysis of potato pulp by a complex enzyme mixture
AU - Bader, J.
AU - Bellgardt, K. H.
AU - Schügerl, K.
N1 - Funding Information: J B gratefully acknowledges financial assu&nce from Stiftung Stlpendlenfonds der Verbandes der Chemlschen Industne (FCI), Germany and the support of Professor H. Voss, Instltut fur Blotechnologie der Rheuusch-Westfahschen Techmschen Hochs-chule Aachen
PY - 1993/8
Y1 - 1993/8
N2 - The enzymatic hydrolysis of potato pulp by a cell-free culture filtrate of Trichoderma reesei Rut C30 was studied. On the basis of the experimental data a dynamic unstructured model using Michaelis-Menten kinetics was developed. This mathematical model describes the enzymatic hydrolysis in terms of the adsorption and desorption of enzymes on the solid substrate and with regard to competitive and uncompetitive inhibition. The model equations consist of a non-linear system of ordinary differential and algebraic equations. Parameter identification was done by dividing the model into submodels and fitting these to experimental data. The simulation results with the model correspond well with the experimental data. Thus the good agreement between simulated and measured process variables indicates that the model is suitable for description of the enzymatic hydrolysis. Computations for different operational conditions show the range of validity and performance of the model. Possibilities for improvements in yield and productivity could be deduced by model computations.
AB - The enzymatic hydrolysis of potato pulp by a cell-free culture filtrate of Trichoderma reesei Rut C30 was studied. On the basis of the experimental data a dynamic unstructured model using Michaelis-Menten kinetics was developed. This mathematical model describes the enzymatic hydrolysis in terms of the adsorption and desorption of enzymes on the solid substrate and with regard to competitive and uncompetitive inhibition. The model equations consist of a non-linear system of ordinary differential and algebraic equations. Parameter identification was done by dividing the model into submodels and fitting these to experimental data. The simulation results with the model correspond well with the experimental data. Thus the good agreement between simulated and measured process variables indicates that the model is suitable for description of the enzymatic hydrolysis. Computations for different operational conditions show the range of validity and performance of the model. Possibilities for improvements in yield and productivity could be deduced by model computations.
UR - http://www.scopus.com/inward/record.url?scp=0027639456&partnerID=8YFLogxK
U2 - 10.1016/0300-9467(93)80045-P
DO - 10.1016/0300-9467(93)80045-P
M3 - Article
AN - SCOPUS:0027639456
VL - 52
SP - B13-B19
JO - The Chemical Engineering Journal
JF - The Chemical Engineering Journal
SN - 0300-9467
IS - 1
ER -