Abstract
The transesterification of methyl acrylate telomers by lipase catalysis in toluene at 50°C was investigated. The specificity of the enzymatic catalyst led to modification of the ester functions of peculiar monomer units. Due to the influence of the near-neighbourhood, only the ester functions of the end-groups and those of the monomer units linked to the telogen segment were modified. It was a completely new result with respect to previous work done in our laboratory. The very precise action of the biocatalyst was characterized from the study of the modification of short telomers as models for longer chains. A detailed analysis of these compounds was made by spectrometric measurements, proton NMR spectroscopy, and size exclusion chromatography. The enzymatic modification opens up numerous possibilities for the design of new acrylate polymers according to the structures of the telogen and of the alcohol used in the transesterification.
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