Abstract
The regio and enantioselectivity of a recombinant cutinase from Fusarium solani pisi was tested on three racemic and one prochiral phenylalkanediols via irreversible transesterification with vinyl acetate. The optimization of the reaction conditions involved the screening of different organic solvents as well as the variation of the substrate concentrations. Thus, the enzymatic activity was checked by measuring initial reaction rates, overall yields, and enantiomeric excess of the reaction products. Only the smaller molecules were recognized by the enzyme, and a denaturing effect of the acyl donor was observed. Nevertheless, a stabilising effect on the enzyme caused by a pre-incubation with the diol was also noted.
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