Figures & data
Figure 1. Chromatography of LOX on gel filtration and Q-Sepharose. (a) The chromatogram of Sephadex G-100 gel filtration. The sample was eluted at a flow rate of 0.25 ml.min−1. The fraction of evaluation based on OD 280 and enzyme activity. (b) Separation of sesame LOX by ion-exchange chromatography on Q-Sepharose column at a flow rate of 1 ml.min−1 using 20 mM Tris-HCL buffer, pH 8.8, as the eluting buffer with a linear gradient of 0.1–1.0 M NaCl. 2 ml fractions were collected. Blue line indicates lipoxygenase activity; red line represents absorbance at 280 nm.
Table 1. Summary of lipoxygenase purification data from Sesamum indicum.
Figure 2. SDS-PAGE of LOX. Lane 1, standard molecular weight proteins (kDa) and lane 2, LOX purified.
Figure 3. pH activity and pH stability of the LOX extracted from sesame seed. (a) pH activity of purified LOX enzyme. (b) Effect of pH on the stability of lipoxygenase enzyme.
Figure 4. (a) Effect of temperature on the activity profile for purified LOX from sesame seed. (b) Thermal stability of purified sesame lipoxygenase.
Figure 5. Arrhenius plot to determine the activation energy for LOX activity of sesame seed when using linoleic acid as a substrate.
Figure 6. Some properties of the enzyme. (a) Lineweaver–Burk plot of the purified lipoxegenase from sesame seed. (b) Relative LOX activity in the presence of chelators such as EDTA and 1,10 phenanthroline. (c) The effect of organic solvents on LOX activity and (d) the effect of different metal ions on LOX activity.
Table 2. The effect of various detergents on LOX activity.