Isolation and Characterisation of a High-Efficiency Desaturase and Elongases from Microalgae for Transgenic LC-PUFA Production
Autor: | Stan S. Robert, Susan I. Blackburn, Anne Maree Mackenzie, Maged P. Mansour, Qing Liu, Dion Matthew Frederick Frampton, Pushkar Shrestha, Peter D. Nichols, James Robertson Petrie, Surinder P. Singh |
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Rok vydání: | 2009 |
Předmět: |
Fatty Acid Desaturases
Linolenic acid Linoleic acid Molecular Sequence Data Saccharomyces cerevisiae Biology Applied Microbiology and Biotechnology chemistry.chemical_compound Acetyltransferases Chlorophyta Microalgae Amino Acid Sequence Transgenes Phylogeny Plant Proteins chemistry.chemical_classification Substrate (chemistry) Eicosapentaenoic acid Yeast Enzyme chemistry Biochemistry Fatty Acids Unsaturated Docosapentaenoic acid Sequence Alignment Polyunsaturated fatty acid |
Zdroj: | Marine Biotechnology. 12:430-438 |
ISSN: | 1436-2236 1436-2228 |
Popis: | The production of long-chain polyunsaturated fatty acids from precursor molecules linoleic acid (LA; 18:2omega6) and alpha-linolenic acid (ALA; 18:3omega3) is catalysed by sequential desaturase and elongase reactions. We report the isolation of a front-end Delta6-desaturase gene from the microalgae Ostreococcus lucimarinus and two elongase genes, a Delta6-elongase and a Delta5-elongase, from the microalga Pyramimonas cordata. These enzymes efficiently convert their respective substrates when transformed in yeast (39-75% conversion for omega3 substrate fatty acids), and the Delta5-elongase in particular displays higher elongation efficiency (75% for conversion of eicosapentaenoic acid (20:5omega3) to docosapentaenoic acid (22:5omega3)) than previously reported genes. In addition, the Delta6-desaturase is homologous with acyl-CoA desaturases and shows a strong preference for the omega3 substrate ALA. |
Databáze: | OpenAIRE |
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