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 $35sim75%$ 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 $60^{circ}C$. The highest activity was found at $45^{circ}C$, 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 $mu M$ level suggesting that the enzyme was Fe ion dependent haloperoxidase.