Abstract
The extracellular activity ofAspergillus niger phytase at the end of the growth phase was 132 nkat/mL in a laboratory bioreactor. The purified enzyme has molar mass approximately 100 kDa, pH optimum at 5.0, temperature optimum at 55°C and high pH and temperature stability. TheK m for dodecasodium phytate, calcium phytate and 4-nitrophenyl phosphate are 0.44, 0.45 and 1.38 mmol/L, respectively. The enzyme is noncompetively inhibited by inorganic monophosphate (K i=2.85 mmol/L) and by Cu2+, Zn2+, Hg2+, Sn2+, Cd2+ ions and strongly by F− ones; it is activated by Ca2+, Mg2+ and Mn2+ ions. The substrate specificity of phytase is broad with the highest affinity to calcium phytate.
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Dvořáková, J., Volfová, O. & Kopecký, J. Characterization of phytase produced byAspergillus niger . Folia Microbiol 42, 349–352 (1997). https://doi.org/10.1007/BF02816948
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DOI: https://doi.org/10.1007/BF02816948