Fig. 2 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 2. Size exclusion chromatography (SEC) profiles of affinity chromatography purified wild-type and mutant proteins. The chromatography was performed on a HiLoad Superdex column 200 PG. Detection was at 280 nm. (A) PmSTSΔ24 WT, (B) PmSTSΔ24 V466E, (C) PmSTSΔ24 W286A, (D) PmSTSΔ24 Y390S, (E) PmSTSΔ24L454A, (F) PmSTSΔ24L454G, and (G) PmSTSΔ24Y390S/L454G were run over a size exclusion column to verify the oligomeric status of generated proteins. Elution profiles of β-sesquiphellandrene synthase proteins are represented together with protein standard: bovine thyroglobulin (670 kDa), bovine gamma globulin (158 kDa), ovalbumin (44 kDa), myoglobin (17 kDa), vitamin B12 (1.35 kDa). The peaks eluted at ~48 mL correspond to protein aggregated during the purification process, and peaks eluted at ~80 mL correspond to the monomeric size of PmSTSΔ24 protein (65 kDa).