Lipase-Catalyzed Enantiomer Selective Hydrolysis of 1,2-Diol Diacetates
Enantiomer selective hydrolysis of racemic 1,2-diol diacetates (rac-2a-h) was investigated by using the inexpensive commercial porcine pancreatic lipase.The hydrolysis proceeds with variable regioselectivity but with moderate to good enantioselectivity yielding a mixture of isomeric monoacetates (3a-h and 4a-h) and unchanged diacetate enantiomers (2a-h).Evidence was found that both monoacetates (3a-h and 4a-h) are formed with the same sense of enantiomer selectivity.