Fig. 5: Physaria fendleri triacylglycerol lipase-like 1 (TAGL1) encodes triacylglycerol lipase activity. | Nature Communications

Fig. 5: Physaria fendleri triacylglycerol lipase-like 1 (TAGL1) encodes triacylglycerol lipase activity.

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

Fig. 5

SDS-PAGE gel (A) and western blot (B) with anti-(His)6x antibody showing the purified His-tagged TAGL1 protein from E. coli. Lane 1, elution fraction from Uninduced cells; Lane 2, purified TAGL1 protein; and Lane M, marker. C TAG lipase activity of purified TAGL1 protein. Experiments A–C were repeated twice independently with similar results. Phosphor image TLC of in vitro lipase assay reactions with [14C]triolein as substrate. Lipase from Rhizopus mehei was used as positive control. Elution fraction from Induced cells, heat-inactivated (H.I.) TAGL1 and no enzyme addition were used as negative controls. The effect of pH (D), time (E), and protein concentration (F) on the rate of [14C]triolein hydrolysis by TAGL1. The amount of substrate used was 5 nmol. All the results were expressed as mean ± SD of two independent experiments. Source data underlying D–F are provided in the source data file.

Back to article page