Substrate selectivity of various lipases in the esterification of cis- and trans-9-octadecenoic acid |
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Authors: | R. Borgdorf S. Warwel |
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Affiliation: | (1) Institute for Biochemistry and Technology of Lipids, H.P. Kaufmann Institute, Federal Centre for Cereal, Potato and Lipid Research, Piusallee 68, D-48147 Münster, Germany e-mail: ibtfett@uni-muenster.de Tel.: +49-251-44073 Fax: +49-251-519275, DE |
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Abstract: | The substrate selectivity of numerous commercially available lipases from microorganisms, plants and animal tissue towards 9-octadecenoic acids with respect to the cis/trans configuration of the CC double bond was examined by the esterification of cis- and trans-9-octadecanoic acid (oleic and elaidic acid respectively) with n-butanol in n-hexane. A great number of lipases studied, e.g. those from Pseudomonas sp., porcine pancreas or Carica papaya, were unable to discriminate between the isomeric 9-octadecenoic acids. However, lipases from Candida cylindracea and Mucor miehei catalysed the esterification of oleic acid 3–4 times faster than the corresponding reaction of elaidic acid and therefore have a high preference for the cis isomer. Of all biocatalysts examined, only recombinant lipases from Candidaantarctica favoured elaidic acid as substrate. While the preference of Candida antarctica lipase B for the trans isomer was quite low, Candida antarctica lipase A had an extraordinary substrate selectivity and its immobilized enzyme preparation [Chirazyme L-5 (3) from Boehringer] esterified elaidic acid about 15 times faster than oleic acid. Received: 29 October 1998 / Received revision: 18 December 1998 / Accepted: 21 December 1998 |
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