Abstract
AbstractA thermo‐unstable hydroxylase was isolated from a Rhodococcus sp. BPG‐8. Activity for the partially purified hydroxylase was enhanced and stabilized in the presence of FAD and catalase. The Vmax values for the oxidation of NADH was 0.28 μmoles · min−1 · mg−1 protein and Km value was 8.3 μM in the presence of these compounds, while in their absence the Vmax value was reduced to 0.09 μmoles · min−1 · mg−1 protein while the Km value changed to 16.1 μM. Resorcinol hydroxylase activity was optimal at pH 7.0, and 25° C. The optimal substrate concentrations were 68 μM and 125 μM in the presence and absence of FAD/catalase, respectively. Chloride ion, and metal ions inhibited the resorcinol hydroxylase activity. The resorcinol hydroxylase utilized various other substrates, and did not influence the hydroxylase activity in the presence of resorcinol.
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