CHARACTERIZATION OF THE RHODOCOCCUS SP BPG-8 RESORCINOL HYDROXYLASE

A thermo-unstable hydroxylase was isolated from a Rhodococcus sp. BPG- 8. Activity for the partially purified hydroxylase was enhanced and st abilized in the presence of FAD and catalase. The V(max) values for th e oxidation of NADH was 0.28 mumoles . min-1 . mg-1 protein and K(m) v alue was 8.3 mum in the presence of these compounds, while in their ab sence the V(max) value was reduced to 0.09 mumoles . min-1 . mg-1 prot ein while the K(m) value changed to 16.1 muM. Resorcinol hydroxylase a ctivity was optimal at pH 7.0, and 25-degrees-C. The optimal substrate concentrations were 68 muM and 125 muM in the presence and absence of FAD/catalase, respectively. Chloride ion, and metal ions inhibited th e resorcinol hydroxylase activity. The resorcinol hydroxylase utilized various other substrates, and did not influence the hydroxylase activ ity in the presence of resorcinol.