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Stereoselective hydrolysis of triglycerides by animal and microbial lipases

Authors

  • Ewa Rogalska,

    1. Centre de Biochimie et de Biologie MoléeAculaire du Centre National de la Recherche Scientifique, Marseille, France
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  • Claire Cudrey,

    1. Centre de Biochimie et de Biologie MoléeAculaire du Centre National de la Recherche Scientifique, Marseille, France
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  • Francine Ferrato,

    1. Centre de Biochimie et de Biologie MoléeAculaire du Centre National de la Recherche Scientifique, Marseille, France
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  • Dr. Robert Verger

    Corresponding author
    1. Centre de Biochimie et de Biologie MoléeAculaire du Centre National de la Recherche Scientifique, Marseille, France
    • Centre de Biochimie et de Biologie MoléeAculaire du Centre National de la Recherche Scientifique, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 09, France
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Abstract

In the present paper, a study on the stereoselectivity of 25 lipases of animal and microbial origin towards homogeneous prochiral triglycerides is presented. All the lipases tested catalyse the hydrolysis of the chemically alike but sterically nonequivalent ester groups in trioctanoin and triolein with different degrees of stereobias, depending on the fatty acyl chain length of the substrate (Rogalska et al., J. Biol. Chem. 256:20271–20276, 1990). Hydrolysis of the sn-2 ester group is catalysed by very few lipases and only Candida antarctica A shows a clear preference for this position. Most of the lipases investigated (12 with trioctanoin and 16 with triolein) showed a preference for the sn-1 position. Using trioctanoin as substrate we observed a total stereoselectivity for position sn-1 with Pseudomonas sp. and Pseudomonas aeruginosa and for position sn-3 with Candida antarctica B. This was not the case with triolein as substrate. Among the 23 lipases studied here and the other two lipases described previously (Rogalska et al., J. Biol. Chem. 256:20271–20276, 1990), 17 show a higher stereoselectivity with trioctanoin than with triolein. With guinea pig pancreatic lipase and with three mold lipases (Geotrichum candidum M, Geotrichum candidum A, and Candida antarctica B), the preference switches from sn-3 to sn-1 when the acyl chain length increases from eight to 18 carbon atoms. The main conclusion to emerge from the present study is that the specific stereopreference of each lipase for a given substrate under given lipolytic conditions can be said to be its fingerprint. © 1993 Wiley-Liss, Inc.

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