Scherkus, ChristianChristianScherkusSchmidt, SandySandySchmidtBornscheuer, Uwe TheoUwe TheoBornscheuerGröger, HaraldHaraldGrögerKara, SelinSelinKaraLiese, AndreasAndreasLiese2019-08-212019-08-212017-02-23Biotechnology and Bioengineering 6 (114): 1215-1221 (2017-06-01)http://hdl.handle.net/11420/3155A 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. © 2017 Wiley Periodicals, Inc.en0006-35922017612151221Wileycomputer simulationenzymatic cascadesoxidoreductasesreaction engineeringϵ-caprolactoneChemieIngenieurwissenschaftenJournal Article10.1002/bit.26258Other