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Investigation of the enzyme-catalysed transesterification of methyl acrylate and sterically hindered alcohol substrates
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| Abstract |
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| For industrial production of valuable building blocks, the use of enzymes as green catalysts has gained a lot of interest recently. In this paper, research on the enzymatic transesterification of methyl esters with different alcohols for the production of high valuable monomers is presented. After screening for the most suitable enzyme catalyst, the influence of the molecular structure of both substrates on the reaction kinetics was investigated. For the best performing substrate, the reaction was optimised. Novozym 435 displays the highest activity for linear as well as for bulkier substrates and has therefore been chosen for the optimisation experiments. Enzymatic transesterification with highly branched and bulky alcohol substrates (e.g. 2-hexyl-l-decanol) resulted in much lower conversion and reaction rates compared to linear and shorter substrates (e.g. octanol). Similar effects were observed when various methyl ester substrates were compared. Furthermore, it was observed that a molar substrate ratio of 3:1 methyl acrylate to alcohol and a substrate to enzyme ratio of 0.1 mol.g(-1) resulted in an optimal conversion. It was also found that reactions using nonpolar solvents (e.g. hexane, heptane, toluene) reached the highest conversion rates. Generally, it can be concluded that enzymatic synthesis of highly specific and bulky alkyl acrylates is possible. However, the structures of both the alcohol and acrylate substrate have an important impact on the reaction rate. |
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English
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ChemistrySelect. - - | |
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2018
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2365-6549 [online]
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3:18(2018), p. 5169-5175
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000432225900024
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