Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase

5Citations
Citations of this article
17Readers
Mendeley users who have this article in their library.
Get full text

Abstract

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.

Cite

CITATION STYLE

APA

Solé, J., Brummund, J., Caminal, G., Schürman, M., Álvaro, G., & Guillén, M. (2019). Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase. ChemCatChem, 11(19), 4862–4870. https://doi.org/10.1002/cctc.201901090

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free