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The biochemical mechanisms of resistance to several heavy metals, which are associated with their accumulation (binding by high-affinity chelating molecules such as thiol-compounds together with their compartmentalization into organelles), are analyzed for the photosynthetic, free-living protist Euglena gracilis. The complete understanding of these mechanisms may facilitate the rational design of strategies for bioremediation of heavy metal polluted water and soil systems. [ABSTRACT FROM AUTHOR]

The free-living protist Euglena gracilis showed an enhanced growth when cultured in the dark with high concentrations of ethanol as carbon source. In a medium containing glutamate/malate plus 1% ethanol, E. gracilis reached a density of 3 × 107 cells/ml after 100 h of culture, which was 5 times higher than that attained with glutamate/malate or ethanol separately. This observation suggested the involvement of a highly active aldehyde dehydrogenase in the metabolism of ethanol. Purification of the E. gracilis aldehyde dehydrogenase from the mitochondrial fraction by affinity chromatography yielded an enrichment of 34 times and recovery of 33% of the total mitochondrial activity. SDS-PAGE and molecular exclusion chromatography revealed a native tetrameric protein of 160 kDa. Kinetic analysis showed Km values of 5 and 50 μM for propionaldehyde and NAD+, respectively, and a Vm value of 1,300 nmol (min × mg protein)−1. NAD+ and NADH stimulated the esterase activity of the purified aldehyde dehydrogenase. The present data indicated that the E. gracilis aldehyde dehydrogenase has kinetic and structural properties similar to those of human aldehyde dehydrogenases class 1 and 2. [ABSTRACT FROM AUTHOR]