Storage Lipid Accumulation and Acyltransferase Action in Developing Flaxseed

January 1, 2005 Human Health and Nutrition Data 0 Comments

Storage Lipid Accumulation and Acyltransferase Action in Developing Flaxseed

Year: 2005
Authors: Sørensen, B.M., Furukawa-Stoffer, T.L., Marshall, K.S., Page, E.K., Mir, Z., Forster, R.J., Weselake, R.J.
Publication Name: Lipids
Publication Details: Volume 40; Pages 1043 – 1049


Investigations of storage lipid synthesis in developing flaxseed (Linum usitatissimum) provide useful information for designing strategies to enhance the oil content and nutritional value of this crop. Lipid content and changes in the FA composition during seed development were examined in two cultivars of flax (AC Emerson and Vimy). The oil content on a dry weight basis increased steadily until about 20 d after flowering (DAF). The proportion of a-linolenic acid (a-18:3, 18:3cisΔ9,12,15) in TAG increased during seed development in both cultivars while the proportions of linoleic acid (18:2cisΔ9,12) and saturated FA decreased. The developmental and substrate specificity characteristics of microsomal DAG acyltransferase (DGAT, EC and lysophosphatidic acid acyltransferase (LPAAT, EC were examined using cultivar AC Emerson. The maximal acyltransferase specific activities occurred in the range of 8–14 DAF, during rapid lipid accumulation on a per seed basis. Acyl-CoA of EPA (20:5cisΔ5,8,11,14,17) or DHA (22:6 cis4,7,10,13,16,19) were included in the specificity studies. DGAT displayed enhanced
specificity for a-18:3-CoA, whereas the preferred substrate of LPAAT was 18:2-CoA. Both enzymes could use EPA- or DHACoA to varying extents. Developing flax embryos were able to take up and incorporate these nutritional FA into TAG and other intermediates in the TAG-formation pathway. This study suggests that if the appropriate acyl-CoA-dependent desaturation/elongation pathways are introduced and efficiently  expressed in flax, this may lead to the conversion of a-18:3-CoA into EPA-CoA, thereby providing an activated substrate for TAG formation. Author's Abstract.

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