Dephosphorylation of Phytate by Using the Aspergillus niger Phytase with a High Affinity for Phytate
Copyright policy )Dephosphorylation of Phytate by Using the Aspergillus niger Phytase with a High Affinity for Phytate
ABSTRACT A phytase (EC 3.1.3.8 ) with a high affinity for phytic acid was found in Aspergillus niger SK-57 and purified to homogeneity in four steps by using ion-exchange chromatography (two types), gel filtration, and chromatofocusing. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme gave a single stained band at a molecular mass of approximately 60 kDa. The Michaelis constant of the enzyme for phytic acid (18.7 ± 4.6 μM) was statistically analyzed. In regard to the orthophosphate released from phytic acid, a significant difference between a low K m phytase from A. niger SK-57 and a high K m phytase from Aspergillus ficuum was recognized.
6-Phytase, Kinetics, Phytic Acid, Aspergillus niger, Hydrogen-Ion Concentration, Phosphorylation
6-Phytase, Kinetics, Phytic Acid, Aspergillus niger, Hydrogen-Ion Concentration, Phosphorylation
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