Fig. 3 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 3. Analysis of monomeric fraction of PmSTS Wild Type and mutant proteins using (A) 12% SDS PAGE and (B) 10% Native PAGE. The SDS PAGE showed high purity of PmSTS protein were obtained for wild type and for all mutants except for PmSTSΔ24W286A and PmSTSΔ24Y390S. The native PAGE showed several species of PmSTSΔ24WT, PmSTSΔ24V466E, and PmSTSΔ24Y390S/L454G that can be resolved on a 10% native gel. However, only one species of PmSTSΔ24L454G and PmSTSΔ24L454A was resolved on a 10% native gel. Smearing bands were observed for PmSTSΔ24W286A and PmSTSΔ24Y390S on the 10% native gel, probably due to the low purity as judged by 12% SDS PAGE.