The extracellular activity of Aspergillus 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 degrees C and high pH and temperature stability. The Km 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 (Ki = 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.

Institute of Microbiology Academy of Sciences of the Czech Republic Prague Czech Republic

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Appl Microbiol. 1968 Sep;16(9):1348-51 PubMed

Nature. 1970 Aug 15;227(5259):680-5 PubMed

J Bacteriol. 1982 Sep;151(3):1102-8 PubMed

J Biol Chem. 1949 May;179(1):53-9 PubMed

Folia Microbiol (Praha). 1994;39(6):481-4 PubMed

Prep Biochem. 1988;18(4):459-71 PubMed

Acta Microbiol Pol. 1978;27(1):41-8 PubMed

Anal Biochem. 1976 May 7;72:248-54 PubMed

Prep Biochem. 1987;17(1):63-91 PubMed

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