Aspergillus FicuumPhytase: Partial Primary Structure, Substrate Selectivity, and Kinetic Characterization

Publisher Website
Google Scholar
Abstract
Purified Aspergillus ficuum phytase's partial primary structure and amino acid and sugar composition were elucidated. Determination of kinetic parameters of the enzyme at different pH values and temperatures indicated no significant alteration of the Km for phytate while the Kcmt was affected. The enzyme was able to release more than 512 of the total available P1 from phytate in a 3.0 hr assay at 58°C, but the Kcmt dropped to 15Z of the initial rate. Substrate selectivity studies revealed phytate to be the preferred substrate. The pH optima of phytase was 5.0, 4.0, and 3.0 for phytate, ATP, and polyphosphate, respectively. The enzyme had varied sensitivity towards cations. While Ca±± and Fe±±produced no effect on the catalytic rate of the enzyme, Cu±, Cu±±, Zn±±, and Fe±±± were found to be inhibitory. Mn±± was observed to enhance enzyme activity by 33Z at 50 μM. Known inhibitors of acid phosphatases e. g. L (±)-tartrate, phosphomycin, and sodium fluoride had no effect on enzyme activity.