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Updated: Jul 4, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Stereospecific hydrolysis by soluble and immobilized lipases
J Lavayre1, J Verrier, J Baratti
1Centre de Biochimie et de Biologie Moléculaire du CNRS, 31 chemin Joseph Aiguier, 13274 Marseille Cedex 2, France.
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.
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