The associated procedures being detailed in the materials and methods section. These compounds were evaluated for their capacity to interact with the enzyme, and were used in excess (10 equivalents) relative to DHLc, following the same general conditions. Despite the use of identical conditions, none of these new aromatic acyl donors proved effective for the acylation of DHLc, as no esters were detected. However, some of them underwent hydrolysis into their corresponding carboxylic acids, which was likely attributable to residual water in the reaction medium. This was particularly prominent for vinyl-2-(4-methoxyphenyl) acetate ( ) which experienced complete hydrolysis, and to a lesser extent for vinyl-4formylbenzoate (11) and vinyl-4-nitrobenzoate (12), exhibiting over 50 % hydrolysis. The lipase A from Candida antarctica and a lipase from Pseudomonas cepacia were also tested with compounds 9 and 12, but both failed to catalyse the desired acylation reaction (data not shown). These results are not entirely surprising, as several lipases have already been tested on other occasions with aromatic acyl donors and have typically demonstrated poor activity. Such is the case for CAL-B, for which another article mentions its inability to catalyse transesterification reactions with phenyl vinyl esters as acyl donors. Consequently, future research may necessitate the identification of a specific enzyme capable of accepting such vinyl esters as acyl donors.