Substrate selectivity of various lipases in the esterification of cis- and trans-9-octadecenoic acid.
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 C=C 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 Candida antarctica 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.
Borgdorf
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Institute for Biochemistry and Technology of Lipids, H.P. Kaufmann Institute, Federal Centre for Cereal, Potato and Lipid Research, Münster, Germany.
Warwel
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S
D001419:Bacteria / Q000201:enzymology; D004951:Esterification; D005658:Fungi / Q000201:enzymology; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D019301:Oleic Acid / Q000737:chemistry / Q000378:metabolism*; D009829:Oleic Acids; D010944:Plants / Q000201:enzymology; D013237:Stereoisomerism; D013379:Substrate Specificity
D009829:Oleic Acids; D019301:Oleic Acid; C011459:elaidic acid; D008049:Lipase