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Ketoisophorone Synthesis with an Immobilized Alcohol Dehydrogenase
Author(s) -
Solé Jordi,
Brummund Jan,
Caminal Glòria,
Schürman Martin,
Álvaro Gregorio,
Guillén Marina
Publication year - 2019
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201901090
Subject(s) - isophorone , chemistry , alcohol dehydrogenase , biocatalysis , yield (engineering) , dehydrogenase , cofactor , organic chemistry , carvone , acetone , nuclear chemistry , alcohol , enzyme , chromatography , catalysis , limonene , reaction mechanism , materials science , essential oil , metallurgy
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.