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Characterization of the Rhodococcus sp. BPG‐8 resorcinol hydroxylase
Author(s) -
Armstrong S. M.,
Patel T. R.
Publication year - 1993
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620330202
Subject(s) - resorcinol , chemistry , catalase , enzyme , substrate (aquarium) , specific activity , nuclear chemistry , biochemistry , organic chemistry , biology , ecology
A 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 V max values for the oxidation of NADH was 0.28 μmoles · min −1 · mg −1 protein and K m value was 8.3 μ M in the presence of these compounds, while in their absence the V max value was reduced to 0.09 μmoles · min −1 · mg −1 protein while the K m value changed to 16.1 μ M . Resorcinol hydroxylase activity was optimal at pH 7.0, and 25° C. The optimal substrate concentrations were 68 μ M and 125 μ M 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.