Biocatalytic synthesis of polymers. Synthesis of an optically active,epoxy-substituted polyester by lipase-catalyzed polymerization

The enantioselective polymerization of bis(2,2,2-trichloroethyl) trans-3,4-epoxyadipate with 1,4-butanediol using the enzyme porcine pancreatic lipase as a catalyst is described. The polymerization was carried out at ambient temperature in anhydrous ethyl ether. End group analysis provided M_N = 5,300 daltons, whereas GPC provided M_w = 7,900 daltons for the polymer. The unchanged (+)-enantiomer of the diester was shown to have an enantiomeric purity of > 95% by proton NMR in the presence of the chiral shift reagent Eu(hfc)₃. The stereochemical purity of the (?)-polymer was estimated at > 96% by consideration of the amount of the slower reacting enantiomer that could have been incorporated and still attain the observed degree of polymerization (25) when the starting ratio of racemic diester to diol was 2:1. Direct determination of the stereochemical purity of the polymer using Eu(hfc)₃ was unsuccessful. Similar studies on polymer having random stereochemical orientations of the epoxide showed that such polymers do not behave as if they are racemic in the presence of the shift reagent. The polymer required for the latter studies was prepared by epoxidation of the product from enzyme catalyzed polymerization of bis(2,2,2-trichloroethyl) trans-3-hexenedioate with 1,4-butanediol.