Details
| Original language | English |
|---|---|
| Pages (from-to) | 1215-1221 |
| Number of pages | 7 |
| Journal | Biotechnology and bioengineering |
| Volume | 114 |
| Issue number | 6 |
| Early online date | 23 Jan 2017 |
| Publication status | Published - 10 Apr 2017 |
| Externally published | Yes |
Abstract
A computational approach for the simulation and prediction of a linear three-step enzymatic cascade for the synthesis of ϵ-caprolactone (ECL) coupling an alcohol dehydrogenase (ADH), a cyclohexanone monooxygenase (CHMO), and a lipase for the subsequent hydrolysis of ECL to 6-hydroxyhexanoic acid (6-HHA). A kinetic model was developed with an accuracy of prediction for a fed-batch mode of 37% for substrate cyclohexanol (CHL), 90% for ECL, and >99% for the final product 6-HHA. Due to a severe inhibition of the CHMO by CHL, a batch synthesis was shown to be less efficient than a fed-batch approach. In the fed-batch synthesis, full conversion of 100 mM CHL was 28% faster with an analytical yield of 98% compared to 49% in case of the batch synthesis. The lipase-catalyzed hydrolysis of ECL to 6-HHA circumvents the inhibition of the CHMO by ECL enabling a 24% higher product concentration of 6-HHA compared to ECL in case of the fed-batch synthesis without lipase. Biotechnol. Bioeng. 2017;114: 1215–1221.
Keywords
- computer simulation, enzymatic cascades, oxidoreductases, reaction engineering, ϵ-caprolactone
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Biotechnology and bioengineering, Vol. 114, No. 6, 10.04.2017, p. 1215-1221.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Kinetic insights into ϵ-caprolactone synthesis
T2 - Improvement of an enzymatic cascade reaction
AU - Scherkus, Christian
AU - Schmidt, Sandy
AU - Bornscheuer, Uwe T.
AU - Gröger, Harald
AU - Kara, Selin
AU - Liese, Andreas
N1 - Funding Information: We are grateful to Deutsche Bundesstiftung Umwelt (DBU) for financial support (AZ 13268).
PY - 2017/4/10
Y1 - 2017/4/10
N2 - A computational approach for the simulation and prediction of a linear three-step enzymatic cascade for the synthesis of ϵ-caprolactone (ECL) coupling an alcohol dehydrogenase (ADH), a cyclohexanone monooxygenase (CHMO), and a lipase for the subsequent hydrolysis of ECL to 6-hydroxyhexanoic acid (6-HHA). A kinetic model was developed with an accuracy of prediction for a fed-batch mode of 37% for substrate cyclohexanol (CHL), 90% for ECL, and >99% for the final product 6-HHA. Due to a severe inhibition of the CHMO by CHL, a batch synthesis was shown to be less efficient than a fed-batch approach. In the fed-batch synthesis, full conversion of 100 mM CHL was 28% faster with an analytical yield of 98% compared to 49% in case of the batch synthesis. The lipase-catalyzed hydrolysis of ECL to 6-HHA circumvents the inhibition of the CHMO by ECL enabling a 24% higher product concentration of 6-HHA compared to ECL in case of the fed-batch synthesis without lipase. Biotechnol. Bioeng. 2017;114: 1215–1221.
AB - A computational approach for the simulation and prediction of a linear three-step enzymatic cascade for the synthesis of ϵ-caprolactone (ECL) coupling an alcohol dehydrogenase (ADH), a cyclohexanone monooxygenase (CHMO), and a lipase for the subsequent hydrolysis of ECL to 6-hydroxyhexanoic acid (6-HHA). A kinetic model was developed with an accuracy of prediction for a fed-batch mode of 37% for substrate cyclohexanol (CHL), 90% for ECL, and >99% for the final product 6-HHA. Due to a severe inhibition of the CHMO by CHL, a batch synthesis was shown to be less efficient than a fed-batch approach. In the fed-batch synthesis, full conversion of 100 mM CHL was 28% faster with an analytical yield of 98% compared to 49% in case of the batch synthesis. The lipase-catalyzed hydrolysis of ECL to 6-HHA circumvents the inhibition of the CHMO by ECL enabling a 24% higher product concentration of 6-HHA compared to ECL in case of the fed-batch synthesis without lipase. Biotechnol. Bioeng. 2017;114: 1215–1221.
KW - computer simulation
KW - enzymatic cascades
KW - oxidoreductases
KW - reaction engineering
KW - ϵ-caprolactone
UR - http://www.scopus.com/inward/record.url?scp=85015317829&partnerID=8YFLogxK
U2 - 10.1002/bit.26258
DO - 10.1002/bit.26258
M3 - Article
C2 - 28112389
AN - SCOPUS:85015317829
VL - 114
SP - 1215
EP - 1221
JO - Biotechnology and bioengineering
JF - Biotechnology and bioengineering
SN - 0006-3592
IS - 6
ER -