Manganese Ion-dependent Production of Phosphodiesterase by Alkalophilic Bacillus No.A-40-2 and Its Properties(Microbiology & Fermentation Industry)

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Phosphodiesterase production with bis-p-nitrophenyl phosphate as a substrate by alkalophilic Bacillus No. A-40-2 increased with increasing Mn^<2+> concentration, showing maximum productivity at 10 mM. The enzyme production was negligible in the medium without Mn^<2+>. The simultaneous addition of 10 mM Mn^<2+> and one of the several cations Mg^<2+>, Co^<2+>, Mo^<6+>, and Pb^<2+> at suitable concentrations stimulated the enzyme production 1.8-fold at most over that with only 10 mM Mn^<2+>. Inorganic phosphate hardly repressed the enzyme production. The enzyme was purified homogeneously. The purified enzyme had the optimum pH of 7.5 and was fairly stable from pH 7-11. The enzyme hydrolyzed 2',3'-cyclic-nucleotides and 3'-nucleotides, but did not hydrolyze 3',5'-cyclic-nucleotides or 5'-nucleotides, indicating it to be a 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16). The enzyme had activity without metals, but Mg^<2+>, Ca^<2+>, Ba^<2+>, and Mo^<6-> activated the enzyme reaction.
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