| Kinetic study of the lipase-catalyzed synthesis of triolein. | |
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MedLine Citation:
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PMID: 18601287 Owner: NLM Status: PubMed-not-MEDLINE |
Abstract/OtherAbstract:
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The kinetics of the synthesis of triolein catalyzed by immobilized Mucor miehei lipase were studied. Equilibrium constants for the synthesis of mono-, di-, and triolein were calculated from the equilibrium compositions for different initial ratios of glycerol and oleic acid by means of multiresponse regression. The 1,3-specific lipase can catalyze the synthesis of triolein because the ester enzymatically formed with the primary alcohol isomerizes, through acyl migration, to an ester on the secondary hydroxyl. The freed primary hydroxyl may then undergo further enzymatic conversion. The rates of isomerization depend on the concentration of oleic acid. |
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Authors:
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R Lortie; M Trani; F Ergan |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biotechnology and bioengineering Volume: 41 ISSN: 0006-3592 ISO Abbreviation: Biotechnol. Bioeng. Publication Date: 1993 May |
Date Detail:
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Created Date: 2008-07-08 Completed Date: 2009-12-14 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7502021 Medline TA: Biotechnol Bioeng Country: United States |
Other Details:
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Languages: eng Pagination: 1021-6 Citation Subset: - |
Affiliation:
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Biotechnology Research Institute, National Research Council, Montréal, Québec, Canada. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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