BIOREMEDIATION OF PHENOLIC-COMPOUNDS FROM WATER WITH PLANT-ROOT SURFACE PEROXIDASES

Peroxidases have been shown to polymerize phenolic compounds, thereby removing them from solution by precipitation. Others have studied the role of root surface associated peroxidases as a defense against fungal root pathogens; however, their use in detoxification of organic pollutants in vivo at the root surface has not been studied. Two plant species, waterhyacinth [Eichhornia crassipes (C. Mart) Solms-Laub.] and tomato (Lycopersicon esculentum L.), were tested for both in vitro and in vivo peroxidase activity on the root surface. In vitro studies indicated that root surface peroxidase activities were 181 and 78 nmol tetraguaiacol formed min-1 g-1 root fresh wt., for tomato and waterhyacinth, respectively. Light microscope studies revealed that guaiacol was polymerized in vivo at the root surface. Although peroxidase was evenly distributed on tomato roots, it was distributed patchily on waterhyacinth roots. In vitro studies using gas chromatography-mass spectrometry (GC-MS) showed that the efficiency of peroxidase to polymerize phenols vary with phenolic compound. We suggest that plants may be utilized as a source of peroxidases for removal of phenolic compounds that are on the EPA priority pollutant list and that root surface peroxidases may minimize the absorption of phenolic compounds into plants by precipitating them at the root surface. In this study we have identified a new use for root-associated proteins in ecologically engineering plant systems for bioremediation of phenolic compounds in the soil and water environment.