Dephosphorylation of phytate by using the Aspergillus niger phytase with a high affinity for phytate.

Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

An extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maxim...

Improved phytate phosphorus utilization by Japanese medaka transgenic for the Aspergillus niger phytase gene.

The inefficient digestion of phytate phosphorus by fish has created environmental concerns associated with phosphorus pollution from aquaculture production facilities. To further complicate this situation, phytate is known to chelate minerals and proteins, making them nutritionally unavailable. The enzyme phytase degrades phytate into inorganic phosphorus, which can be directly utilized by fish...

An in vitro procedure for studying enzymic dephosphorylation of phytate in maize-soyabean feeds for turkey poults.

An in vitro method was developed to predict inorganic P release from maize-soyabean poultry feeds containing supplemental phytase (EC 3.1.3.8), and to quantify the effect of acid phosphatase (EC 3.1.3.2), fungal protease (EC 3.4.23.6) and Aspergillus niger cellulase (EC 3.2.1.4) on phytate dephosphorylation. Pepsin (EC 3.4.23.1) and pancreatin digestion periods were preceded by a 30 min pre-inc...

Utilization of Aspergillus niger Phytase Preparation for Hydrolysis of Phytate in Foods

Isolation of a thermostable acid phytase from Aspergillus niger UFV-1 with strong proteolysis resistance

An Aspergillus niger UFV-1 phytase was characterized and made available for industrial application. The enzyme was purified via ultrafiltration followed by acid precipitation, ion exchange and gel filtration chromatography. This protein exhibited a molecular mass of 161 kDa in gel filtration and 81 kDa in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), indicating that it m...