Fig. 6: Fatty acid selectivity of Physaria fendleri TAGL1. | Nature Communications

Fig. 6: Fatty acid selectivity of Physaria fendleri TAGL1.

From: Identification of triacylglycerol remodeling mechanism to synthesize unusual fatty acid containing oils

Fig. 6

A Competitive lipase assay model. Equimolar amounts (1:1) of 14C-labeled triolein along with either unlabeled triolein (Assay 1) or 1HFA-TAG (Assay 2) or 2HFA-TAG (Assay 3) were used as a substrates. In assays 2–3, if a lipase selectively cleaves oleate over other fatty acids the rate of [14C]triolein degradation will increase compared to 1. However, if the lipase prefers other fatty acids over oleate the rate of [14C]triolein degradation will decrease. Lipase activity of PfeTAGL1 protein was represented as the amount (%) of [14C]triolein degraded (B) and release of [14C]oleic acid (C) as measured by phosphor imaging. Results are shown as Mean ± SD of three independent assay reactions. Means with different letters are significantly different according to the one-way ANOVA with LSD test at p < 0.05. Source data underlying B, C and exact p values are provided in the source data file.

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