Details
| Original language | English |
|---|---|
| Pages (from-to) | 22-30 |
| Number of pages | 9 |
| Journal | Process biochemistry |
| Volume | 88 |
| Early online date | 17 Oct 2019 |
| Publication status | Published - Jan 2020 |
| Externally published | Yes |
Abstract
ε-Caprolactone is an industrially important intermediate produced in multi-10,000 ton scale annually with broad applications. We report on a whole-cell biocatalytic conversion of cyclohexanol to ε-caprolactone using the combination of alcohol dehydrogenase (ADH) with two stability-improved variants (QM and M15) of the Baeyer-Villiger monooxygenase CHMO with a special focus on process development at the 200 mM scale. Influence of parameters such as volumetric mass transfer co-efficient, stirrer speed and catalytic loading (amount of E. coli whole-cells expressing ADH and CHMO) on the process efficiency were studied and optimised. This resulted in over 98% conversion, a product titer of 20 g L–1 and an isolated product amount of 9.1 g (80%). This corresponds to a space-time yield of 1.1 g L–1 h−1 and a reaction yield (mole of product per mole substrate) of 0.9. Comparing the two CHMO variants a significant difference in catalytic yield (weight of product to weight of catalyst; 0.6 vs 0.3) was observed without any inherent changes in the process. Hence, the reported process can accommodate in the future improved variants of the CHMO.
Keywords
- Alcohol dehydrogenase, Cyclohexanone monooxygenase, Process optimisation, Whole-cell biocatalysis, ε-caprolactone synthesis
ASJC Scopus subject areas
- Chemical Engineering(all)
- Bioengineering
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Process biochemistry, Vol. 88, 01.2020, p. 22-30.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A whole-cell process for the production of ε-caprolactone in aqueous media
AU - Srinivasamurthy, Vishnu S.T.
AU - Böttcher, Dominique
AU - Engel, Jennifer
AU - Kara, Selin
AU - Bornscheuer, Uwe T.
N1 - Funding Information: The authors would like to thank Mr. Frederic Perz (Institute of Technical Biocatalysis, Hamburg University of Technology, Germany) for help with the preparation of process flow diagram with Aspen software and Dr. Diederik J. Opperman (Department of Biotechnology, University of the Free State, South Africa) for sharing CHMO M15.
PY - 2020/1
Y1 - 2020/1
N2 - ε-Caprolactone is an industrially important intermediate produced in multi-10,000 ton scale annually with broad applications. We report on a whole-cell biocatalytic conversion of cyclohexanol to ε-caprolactone using the combination of alcohol dehydrogenase (ADH) with two stability-improved variants (QM and M15) of the Baeyer-Villiger monooxygenase CHMO with a special focus on process development at the 200 mM scale. Influence of parameters such as volumetric mass transfer co-efficient, stirrer speed and catalytic loading (amount of E. coli whole-cells expressing ADH and CHMO) on the process efficiency were studied and optimised. This resulted in over 98% conversion, a product titer of 20 g L–1 and an isolated product amount of 9.1 g (80%). This corresponds to a space-time yield of 1.1 g L–1 h−1 and a reaction yield (mole of product per mole substrate) of 0.9. Comparing the two CHMO variants a significant difference in catalytic yield (weight of product to weight of catalyst; 0.6 vs 0.3) was observed without any inherent changes in the process. Hence, the reported process can accommodate in the future improved variants of the CHMO.
AB - ε-Caprolactone is an industrially important intermediate produced in multi-10,000 ton scale annually with broad applications. We report on a whole-cell biocatalytic conversion of cyclohexanol to ε-caprolactone using the combination of alcohol dehydrogenase (ADH) with two stability-improved variants (QM and M15) of the Baeyer-Villiger monooxygenase CHMO with a special focus on process development at the 200 mM scale. Influence of parameters such as volumetric mass transfer co-efficient, stirrer speed and catalytic loading (amount of E. coli whole-cells expressing ADH and CHMO) on the process efficiency were studied and optimised. This resulted in over 98% conversion, a product titer of 20 g L–1 and an isolated product amount of 9.1 g (80%). This corresponds to a space-time yield of 1.1 g L–1 h−1 and a reaction yield (mole of product per mole substrate) of 0.9. Comparing the two CHMO variants a significant difference in catalytic yield (weight of product to weight of catalyst; 0.6 vs 0.3) was observed without any inherent changes in the process. Hence, the reported process can accommodate in the future improved variants of the CHMO.
KW - Alcohol dehydrogenase
KW - Cyclohexanone monooxygenase
KW - Process optimisation
KW - Whole-cell biocatalysis
KW - ε-caprolactone synthesis
UR - http://www.scopus.com/inward/record.url?scp=85074477884&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2019.10.009
DO - 10.1016/j.procbio.2019.10.009
M3 - Article
AN - SCOPUS:85074477884
VL - 88
SP - 22
EP - 30
JO - Process biochemistry
JF - Process biochemistry
SN - 1359-5113
ER -