The activity of geranyl pyrophosphate (GPP) synthase of several cyanobacteria has been evaluated by thin layer chromatography (TLC) and liquid scintillation counter. Two kinds of Phormidium tenue (P. tenue) wild strains and two kinds of pure strains P. tenue and Oscillatoria limnetica (O. limnetica) were used in the experiments. Harvested cells were disrupted by ultrasonic and ultracentrifuged at 100,000 X g for 60 min at 4°C. The supernatant and pellet were used for GPP synthase assay. GPP synthase activity was first determined from P. tenue. The highest enzymatic activity was observed in the supernatant ultracentrifuged at 100,000 X g, therefore this enzyme was present in the cytoplasm. The supernatant was fractionated by ammonium sulfate and the enzymatic activity of 30% ammonium sulfate fractionation was twice the strength compared with and without ammonium sulfate fractionation. 2-Methylisoborneol (MIB) production did not correspond to the activity of GPP synthase as determined by the comparison of enzymatic activity between odor producing and non-producing strains.

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