Kinetic insights into E-caprolactone synthesis: Improvement of an enzymatic cascade reactionScherkus, C., Schmidt, S., Bornscheuer, U. T., Groeger, H., Kara, S. & Liese, A., Jun-2017, In : Biotechnology and Bioengineering. 114, 6, p. 1215-1221 7 p.
Research output: Contribution to journal › Article › Academic › peer-review
A computational approach for the simulation and prediction of a linear three-step enzymatic cascade for the synthesis of E-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 100mM 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. (c) 2017 Wiley Periodicals, Inc.
|Number of pages||7|
|Journal||Biotechnology and Bioengineering|
|Publication status||Published - Jun-2017|
- E-caprolactone, enzymatic cascades, oxidoreductases, reaction engineering, computer simulation, BAEYER-VILLIGER-MONOOXYGENASES, EPSILON-CAPROLACTONE, CYCLOHEXANONE MONOOXYGENASE, DEHYDROGENASE, REGENERATION, OXIDATION, DESIGN