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KMID : 0364820080440020116
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Korean Journal of Microbiology
2008 Volume.44 No. 2 p.116 ~ p.121
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Screening and Partial Purification of Haloperoxidase from Marine Actinomycetes
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Cho Ki-Woong
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Abstract
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In my search of microbial source of novel enzymes, a marine actinomycetes, A1460, producing haloperoxidase
was isolated from macroalgae from south sea, Korea and studied for physiological and biochemical properties.
The haloperoxidation reaction was followed by the bromination of phenol red in the presence of hydrogen peroxide
and potassium bromide. The haloperoxidase was partially purified from the cell extract with 35~75%
ammonium sulfate precipitation, High-Q anion exchange chromatography, gel filtration chromatography,
hydroxyapetite chromatography and hydrophobic interaction chromatography to a yield of 42% and purification
fold of 70. This enzyme showed relatively high heat stability without losing 50% of activity after 1 hr incubation
at 60oC. The highest activity was found at 45oC, and the optimal pH was about pH 7, but higher stability was
observed at pH 8. Azide and cyanide ion showed strong inhibition at less than 1 μM level suggesting that the
enzyme was Fe ion dependent haloperoxidase.
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KEYWORD
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haloperoxidase, marine actinomycetes, thermostable
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