Stereospecific hydrolysis by soluble and immobilized lipases

Abstract

Stereospecific hydrolysis of insoluble monoesters by lipases are reported. Among the lipases tested, porcine pancreatic lipase was the most stereospecific when acting on 3‐chloro–2‐methyl propanol propionate. When the chain length of the acid was enhanced, the stereospecificity decreased. Initial rate measurements analysis concluded that the observed stereospecificity was the result of different catalytic constants rather than different Michaelis constants. From these results, methods were derived for the preparation of l‐ or d‐3‐chloro–2‐methylpropanol (an intermediary in the synthesis of levomepromasine) based on the hydrolysis of esters by soluble or immobilized lipases.