Isolation, purification, and partial characterization of plant dehalogenase-like activity from waterweed (elodea canadensis)

摘要

Plants have been shown to effectively degrade halogenated contaminants. This is the first report of a dehalogenase-like activity isolated and purified from plants. This activity is suspected to be cofactor of a dehalogenase. The putative cofactor is heat stable, has broad pH stability, and is protease resistant. It is soluble in methanol, active both in aerobic and anaerobic conditions and has a broad substrate specificity with a pH optima of pH 8.5. The activity is completely inhibited by EDTA and requires ascorbate as teh electron donor. An analytical methodology has been devleoped to isolate and purify the cofactor as well as to quantify the cofactor dehalogenase-like activity.