Abstract
A model has been developed to describe the interaction between two enzymes and an intermediary redox mediator. In this bi-enzymatic process, the enzyme cellobiose dehydrogenase oxidizes lactose at the C-1 position of the reducing sugar moiety to lactobionolactone, which spontaneously hydrolyzes to lactobionic acid. 2,20 Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt is used as electron acceptor and is continuously regenerated by laccase. Oxygen is the terminal electron acceptor and is fully reduced to water by laccase, a coppercontaining oxidase. Oxygen is added to the system by means of bubble-free oxygenation. Using the model, the productivity of the process is investigated by simultaneous solution of the rate equations for varying enzyme quantities and redox mediator concentrations, solved with the aid of a numerical solution. The isocharts developed in this work provide an easy-to-use graphical tool to determine optimal process conditions. The model allows the optimization of the employed activities of the two enzymes and the redox mediator concentration for a given overall oxygen mass transfer coefficient by using the isocharts. Model predictions are well in agreement with the experimental data.
| Original language | English |
|---|---|
| Pages (from-to) | 1475-1482 |
| Number of pages | 8 |
| Journal | Biotechnology and Bioengineering |
| Volume | 102 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 1 Apr 2009 |
| Externally published | Yes |
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Keywords
- Biotransformations
- Carbohydrates
- Cellobiose dehydrogenase
- Kinetic modeling
- Laccase
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
Cite this
Kinetic modeling of a bi-enzymatic system for efficient conversion of lactose to lactobionic acid. / Van, Wouter; Bhagwat, Aditya; Ludwig, Roland; Dewulf, Jo; Haltrich, Dietmar; Van Langenhove, Herman.
In: Biotechnology and Bioengineering, Vol. 102, No. 5, 01.04.2009, p. 1475-1482.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Kinetic modeling of a bi-enzymatic system for efficient conversion of lactose to lactobionic acid
AU - Van, Wouter
AU - Bhagwat, Aditya
AU - Ludwig, Roland
AU - Dewulf, Jo
AU - Haltrich, Dietmar
AU - Van Langenhove, Herman
PY - 2009/4/1
Y1 - 2009/4/1
N2 - A model has been developed to describe the interaction between two enzymes and an intermediary redox mediator. In this bi-enzymatic process, the enzyme cellobiose dehydrogenase oxidizes lactose at the C-1 position of the reducing sugar moiety to lactobionolactone, which spontaneously hydrolyzes to lactobionic acid. 2,20 Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt is used as electron acceptor and is continuously regenerated by laccase. Oxygen is the terminal electron acceptor and is fully reduced to water by laccase, a coppercontaining oxidase. Oxygen is added to the system by means of bubble-free oxygenation. Using the model, the productivity of the process is investigated by simultaneous solution of the rate equations for varying enzyme quantities and redox mediator concentrations, solved with the aid of a numerical solution. The isocharts developed in this work provide an easy-to-use graphical tool to determine optimal process conditions. The model allows the optimization of the employed activities of the two enzymes and the redox mediator concentration for a given overall oxygen mass transfer coefficient by using the isocharts. Model predictions are well in agreement with the experimental data.
AB - A model has been developed to describe the interaction between two enzymes and an intermediary redox mediator. In this bi-enzymatic process, the enzyme cellobiose dehydrogenase oxidizes lactose at the C-1 position of the reducing sugar moiety to lactobionolactone, which spontaneously hydrolyzes to lactobionic acid. 2,20 Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt is used as electron acceptor and is continuously regenerated by laccase. Oxygen is the terminal electron acceptor and is fully reduced to water by laccase, a coppercontaining oxidase. Oxygen is added to the system by means of bubble-free oxygenation. Using the model, the productivity of the process is investigated by simultaneous solution of the rate equations for varying enzyme quantities and redox mediator concentrations, solved with the aid of a numerical solution. The isocharts developed in this work provide an easy-to-use graphical tool to determine optimal process conditions. The model allows the optimization of the employed activities of the two enzymes and the redox mediator concentration for a given overall oxygen mass transfer coefficient by using the isocharts. Model predictions are well in agreement with the experimental data.
KW - Biotransformations
KW - Carbohydrates
KW - Cellobiose dehydrogenase
KW - Kinetic modeling
KW - Laccase
UR - http://www.scopus.com/inward/record.url?scp=63549147813&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=63549147813&partnerID=8YFLogxK
U2 - 10.1002/bit.22165
DO - 10.1002/bit.22165
M3 - Article
C2 - 18988269
AN - SCOPUS:63549147813
VL - 102
SP - 1475
EP - 1482
JO - Biotechnology and Bioengineering
JF - Biotechnology and Bioengineering
SN - 0006-3592
IS - 5
ER -