Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

Jordi Solé, Jan Brummund, Glòria Caminal, Martin Schürman, Gregorio Álvaro, Marina Guillén

Research output: Contribution to journalArticleResearch

5 Citations (Scopus)

Abstract

© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim The monoterpenoid α-isophorone is sourced from the available and renewable plant dry matter, as well as a waste recovery operation from acetone. This compound, can be hydroxylated to 4-hydroxy-isophorone which is the main precursor for the synthesis of ketoisophorone. On its turn, ketoisophorone is a key intermediate for the production of carotenoids and Vitamin E. Here, the enzymatic oxidation of 4-hydroxy-isophorone to ketoisophorone is demonstrated employing an alcohol dehydrogenase (ADHaa) from Artemisia annua and a NADPH oxidase (NOX), as a cofactor regeneration enzyme. After 24 h of reaction and an initial substrate concentration of 50 mM, 95.7 % yield and a space time yield of 6.52 g L−1 day−1 could be obtained. Furthermore, the immobilization of the alcohol dehydrogenase was studied on 17 different supports. An epoxy-functionalized agarose resulted in the highest metrics, 100±0% immobilization yield and 58.2±3.5 % retained activity. Finally, the immobilized ADHaa was successfully implemented in 4 reaction cycles (96 h operation) presenting a biocatalyst yield of 23.4 g product g−1 of enzyme. It represents a 2.5-fold increase compared with the reaction with soluble enzymes.
Original languageEnglish
Pages (from-to)4862-4870
Number of pages9
JournalChemCatChem
Volume11
Issue number19
DOIs
Publication statusPublished - 7 Oct 2019

Keywords

  • ALLYLIC OXIDATION
  • ALPHA-ISOPHORONE
  • CHEMICALS
  • CHLORIDE
  • EFFICIENT
  • LIGNOCELLULOSIC BIOMASS
  • PLATFORM
  • SELECTIVE SYNTHESIS
  • STABILIZATION
  • SUPPORT
  • alcohol dehydrogenase
  • biocatalysis
  • immobilization
  • ketoisophorone
  • recycling

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