Title : Biosynthesis of ethyl caproate and other short ethyl esters catalyzed by cutinase in organic solvent - de Barros_2009_J.Mol.Catal.B.Enzym_60_178 |
Author(s) : de Barros DPC , Fonseca LP , Fernandes P , Cabral JMS , Mojovic L |
Ref : J Mol Catal B Enzym , 60 :178 , 2009 |
Abstract :
Abstract: The main objective of this work was to study the enzymatic synthesis of short chain ethyl esters, a group of relevant aroma molecules, by Fusarium solani pisi cutinase in an organic solvent media (iso-octane), and to assess the influence of different parameters on the reaction yield. Cutinase displayed high initial esterification rates in iso-octane, which amounted to 1.15micromolmin-1mg-1 for ethyl butyrate (C4 acid chain) and 1.06micromolmin-1mg-1 for ethyl valerate (C5 acid chain). High product yields, 84% for ethyl butyrate and 96% for ethyl valerate, were observed after 6h of reaction, for an initial equimolar concentration of substrates (0.1M). The highest product yield (97%) was observed for ethyl caproate (C6) synthesis, a compound which is a part of natural apple and pineapple flavour, for an alcohol:acid molar ratio of 2 (0.2M ethanol concentration). Cutinase affinity for short chain length carboxylic acids (C4C6) in ester synthesis in iso-octane confirmed previous observations in reversed micellar system. |
PubMedSearch : de Barros_2009_J.Mol.Catal.B.Enzym_60_178 |
PubMedID: |
de Barros DPC, Fonseca LP, Fernandes P, Cabral JMS, Mojovic L (2009)
Biosynthesis of ethyl caproate and other short ethyl esters catalyzed by cutinase in organic solvent
J Mol Catal B Enzym
60 :178
de Barros DPC, Fonseca LP, Fernandes P, Cabral JMS, Mojovic L (2009)
J Mol Catal B Enzym
60 :178