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A THERMO-STABLE DEHALOGENASE IN THE EXTRACTS FROM PSEUDOMONAS SP (STRAIN-19S)

A thermo-stable dehalogenase was demonstrated in the crude extracts from Pseudomonas sp (19S). The ability of the enzyme to catalyze the dehalogenation of various halogen-substituted organic acids was investigated and the highest activity was found with monochloroacetate. The enzyme followed Michael is-Menten kinetics, and the Km for monochloroacetate was O.2mM. Maximum activity was found at pH 10.5 and 60~ The enzyme activity in the cell-free extract was unaffected by EDTA or by Mn, Zn, or Cu ions, but was dramatically reduced by HgClz (70 %) and Pb (N03)~ (80 %).