Copper Enhanced Monooxygenase Activity and FT-IR Spectroscopic Characterisation of Biotransformation Products in Trichloroethylene Degrading Bacterium: Stenotrophomonas maltophilia PM102
Figure 6
(a) The 8% native PAGE with proteins obtained by lysozyme extraction from PM102 cells grown in minimal medium with 0.2% TCE for 24 hours followed by induction with 0.2% of various carbon sources: TCE, toluene, chloroform, benzene, hexane, and petroleum for another 24 hours. (b) The 8% native gel with protein fractions purified from culture supernatant. As enzyme activity was higher in the supernatant, extracellular proteins were purified by ammonium sulphate precipitation. At 70% ammonium sulphate, the two protein bands that gave activity bands are shown with arrows. (c) The 8% native gel zymogram showing two activity bands lying in close proximity indicating two isoforms of the enzyme.
