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Substrate specificity of the lipase fromCandida parapsilosis

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Lipids

Abstract

Substrate specificity of the acyltransferase activity of the lipase (EC 3.1.1.3) fromCandida parapsilosis CBS 604 was studied in aqueous media. The specificity toward both acid and alcohol parts of a large number of acylglycerols and aliphatic esters was investigated. This lipase showed a high activity in the presence of esters with long-chain fatty acids and particularly unsaturated fatty acids with acis-Δ9 double bond. It was observed that the activity profile depended not only on the alcohol part of the acyl ester, but also on the temperature of the reactant medium. The best lipid substrates had their melting point between −40 to +20°C, 14 to 18 carbon atoms in the acyl group and 1 to 4 carbon atoms in the alkyl group. The enzyme, defined as an acyltransferase in a previous paper, showed a high affinity for primary and secondary alcohols with a short carbon chain (1 to 5 carbon atoms) as acyl acceptors. The influence of free alcohols in the reactant medium on the hydrolysis and alcoholysis activities of the enzyme is discussed. Two phenomena seem to be involved, depending on the alcohol: competition with water for the acyltransfer reaction and lipid substrate dilution when the alcohol places at the oil/water interface.

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Abbreviations

FA:

fatty acid

GC:

gas chromatography

HPLC:

high-performance liquid chromatography

TLC:

thin-layer chromatography

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Authors and Affiliations

  1. Ecole Nationale Supérieure Agronomique, Institut National de la Recherche Agronomique, 34060, Montpellier, France

    Delphine Briand, Eric Dubreucq & Pierre Galzy

  2. Ecole Nationale Supérieure de Chimie, 34053, Montpellier, France

    Jean Grimaud

Authors
  1. Delphine Briand
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  2. Eric Dubreucq
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  3. Jean Grimaud
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  4. Pierre Galzy
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Briand, D., Dubreucq, E., Grimaud, J. et al. Substrate specificity of the lipase fromCandida parapsilosis . Lipids 30, 747–754 (1995). https://doi.org/10.1007/BF02537802

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  • DOI: https://doi.org/10.1007/BF02537802

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