Author(s): Pires-Cabral, P. ; Fonseca, M.M.R. da ; Ferreira-Dias, S.
Date: 2009
Persistent ID: http://hdl.handle.net/10400.5/5997
Origin: Repositório da Universidade de Lisboa
Subject(s): biocatalyst preparation; enzyme; kinetics; lipase; polyurethane foams
A kinetic study on the synthesis of ethyl butyrate in n-hexane, catalyzed by Candida rugosa lipase immobilized in two hydrophilic polyurethane foams (“HYPOL FHP 2002” and “HYPOL FHP 5000”)was performed. With the “FHP5000” foams, esterification rates and conversion were always higher than those obtained with “FHP2002”. For both immobilized preparations, BA did not cause any inhibition on the enzymatic activity, in the range of concentration tested (0.078–0.7M) at an initial ethanol concentration of 0.105M. Michäelis–Menten kinetics was observed: a plateau being reached at the initial bulk BA concentration of 0.40Mand 0.45 M, corresponding to microenvironmental concentrations of 0.851Mand 0.329 M, respectively with the lipase in “FHP2002” and “FHP5000” foams. Inhibition by EtOH was observed for initial bulk concentrations higher than 0.15 M, corresponding to microenvironmental concentrations of 0.426M and 0.256 M, for the lipase in “FHP2002” and “FHP5000” foams, respectively. Kinetic data could be well described by the substrate-inhibition model, considering the initial bulk or microenvironmental ethanol concentrations as inhibitory
