Abstract
Acyltransferase fromMycobacterium smegmatis(MsAcT) immobilised in continuous-flow microchannel reactors with hierarchical pore structure enabled quantitative, full and rapid transesterification of neopentylglycol (NPG) with ethyl acetate in less than one minute.
Highlights
The most recent study of MsAcT's synthetic properties shed light on its application prospects to catalyse reactions in aqueous media.[1]
The experiments revealed that the rate of monoester formation in the microreactor was exceedingly fast compared to that of diester synthesis and the native enzyme behaviour in a batch reactor
NPG is the substrate employed for the activity assay of MsAcT. It is suitable for this study as it is a symmetric diol with two primary hydroxyl groups
Summary
The most recent study of MsAcT's synthetic properties shed light on its application prospects to catalyse reactions in aqueous media.[1]. Continuous-flow systems with very high performance are desirable, in particular since they offer a new handle on reaction engineering.[12] For this reason we deemed it important to undertake studies of the MsAcT behaviour in a continuous-flow transesterification of neopentylglycol (NPG) in a microchannel (micro)reactor. NPG is the substrate employed for the activity assay of MsAcT It is suitable for this study as it is a symmetric diol with two primary hydroxyl groups. This enables a facile flow of reactants and results in intensive mixing and mass transport to the enzyme The latter was immobilised in very large mesopores using two distinctly different immobilisation concepts to improve operational stability and to make use of the protein confinement effect by increasing the surface-to-volume ratio in microreactor technology.[12]
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