Abstract
A novel enzyme, of a Pseudomonas species, was purified by ammonium sulfate fractionation and column chromatographies on DEAE-Toyopearl 650M and Toyopearl HW-55s.The activity recovery was 87% at the ammonium sulfate fractionation step and 44% at the final step of the purification, respectively. The purified enzyme was homogeneous electrophoretically and its molecular weight was 72,000. The optimum pH and temperature were 6.5 and 55°C, respectively. The enzyme was stable up to 45°C in the pH range of 6.5 to 9.0 for 1 hr, and thermostable in the presence of 2 mm CaCl2 up to 50°C. The isoelectric point of the enzyme was 6.5. The enzyme activity was inhibited by metal ions such as Zn2+, Cu2+, Ag+ and Hg2+, and enhanced by Rb+, Mg2+, Co2+ and Ca2+.The enzyme specifically produced maltopentaose from starch in the initial stage of the reaction, finally producing maltose and maltotriose. The enzyme did not act on glucose, maltose or maltotriose, and maltohexaose was considerably resistant to the enzyme’s action. I...
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