Abstract
FMN could be dephosphorylated enzymatically by white strain of Er. ashbyii. In the case of partially purified enzyme from Er. ashbyii, the optimum pH and temperature were found at 9.0 and 55℃, respectively. The enzyme action was inhibited by ethylenediaminetetraacetate, and activated by Mg^<++>. From these results, the enzyme action was considered to be attributed to alkaline phosphomonoesterase. The larger amount of the enzyme was found in white strain than in yellow strain.
