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Hydrolysis of linoleate geometric isomers by Geotrichum candidum lipase
Author(s) -
Jensen Robert G.,
Gordon Dennis T.,
Scholfield C. R.
Publication year - 1973
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02531913
Subject(s) - geotrichum , lipase , hydrolysis , cis–trans isomerism , chemistry , enzyme , biocatalysis , structural isomer , stereochemistry , organic chemistry , food science , catalysis , reaction mechanism
Lipase (EC 3.1.1.3) from the microorganism Geotrichum candidum preferentially hydrolyzes cis ‐9 18∶1 and cis,cis ‐9,12 18∶2 from triacylglycerols, largely ignoring all other positional isomers of cis 18∶1 as well as trans ‐9 18∶1. To obtain additional information about the specificity of the enzyme, two triacylglycerols were prepared and utilized as substrates. The lipase hydrolyzed 85% cis,cis ‐9,12 18∶2 and 15% trans,trans ‐9,12 18∶2 from the triacylglycerol, containing ca. 50% of each acid. From the triacylglycerol containing 46.3% cis,trans ‐9,12 18∶2 and 53.7% trans,cis ‐9,12 18∶2, 44.8 and 55.2% of the two acids were hydrolyzed. Therefore the enzyme discriminated against the trans,trans isomer but not between the cis,trans and trans,cis isomers.