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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-8-14
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pubmed:abstractText |
Laccase enzymes were investigated for their potential to catalyze the oxidation of trilinolein and methyl linoleate. This study demonstrates that laccase enzymes can oxidize unsaturated fatty acid esters and their associated lipids. The reaction products resulting from laccase-catalyzed reactions with trilinolein were analyzed using combined reversed-phase high-performance liquid chromatography and mass spectrometry via an atmospheric pressure chemical ionization source. The dominant oxidation products detected were monohydroperoxides, bishydroperoxides, and epoxides. This paper presents the first detailed investigation into the interaction between laccase enzymes and lipids containing unsaturated fatty acids.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0003-9861
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
405
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44-54
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12176056-Chromatography, Gas,
pubmed-meshheading:12176056-Chromatography, High Pressure Liquid,
pubmed-meshheading:12176056-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12176056-Epoxy Compounds,
pubmed-meshheading:12176056-Fatty Acids,
pubmed-meshheading:12176056-Ions,
pubmed-meshheading:12176056-Laccase,
pubmed-meshheading:12176056-Linoleic Acids,
pubmed-meshheading:12176056-Lipid Metabolism,
pubmed-meshheading:12176056-Mass Spectrometry,
pubmed-meshheading:12176056-Models, Chemical,
pubmed-meshheading:12176056-Oxidoreductases,
pubmed-meshheading:12176056-Platelet Aggregation Inhibitors,
pubmed-meshheading:12176056-Pressure,
pubmed-meshheading:12176056-Spectrophotometry,
pubmed-meshheading:12176056-Time Factors,
pubmed-meshheading:12176056-Triglycerides
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pubmed:year |
2002
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pubmed:articleTitle |
Degradation of trilinolein by laccase enzymes.
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pubmed:affiliation |
Chair of Forest Products Biotechnology, Faculty of Forestry, 4301-2424 Main Mall, The University of British Columbia, Vancouver, BC, Canada V6T 1Z4.
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pubmed:publicationType |
Journal Article
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