Reaction design for evaluation of the substrate range of hydrolases

Biocatalytic acylation reactions involving 24 alcohols, 8 acyl donors and 6 hydrolases were analysed using an original method. The reaction outcome was determined by semi-automated semi-automated solid-phase microextraction and GC/MS (SPME-GC/MS) allowing rapid evaluation of the success rate of each enzyme. Using Candida antarctica Lipase B (CALB), in 36% of the cases (46 reactions) quantitative conversion of the starting alcohol was observed, with an average isolated yield of 96%. The platform was then used to screen other enzymes with the CALB non-reacting substrates, allowing the design and optimisation of some efficient enzymatic reactions. Modification of the odour profile of rose essential oils by enzymatic treatment was also carried out.