Optical Resolution of Unusual Amino-Acids by Lipase-catalysed Hydrolysis
The 2-chloroethyl esters of the N-benzyloxycarbonyl (Z) derivatives of several unusual amino-acids are converted by Aspergillus niger lipase into enantiomerically enriched Z-amino-acids with fairly high optical purities, the L-enantiomers being preferentially hydrolysed.
Porcine Pancreatic Lipase Catalyzed Enantioselective Hydrolysis of Esters of N-Protected Unusual Amino Acids
Porcine pancreatic lipase catalyzed the highly enantioselective hydrolysis of a kind of α-substituted carboxylic esters, i.e., the 2,2,2-trifluoroethyl esters of the N-benzyloxycarbonyl derivatives of unusual amino acids.