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Brazilian Journal of Microbiology

versão impressa ISSN 1517-8382versão On-line ISSN 1678-4405

Resumo

GREINER, Ralf; SILVA, Lucineia Gomes da  e  COURI, Sonia. Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9. Braz. J. Microbiol. [online]. 2009, vol.40, n.4, pp.795-807. ISSN 1517-8382.  https://doi.org/10.1590/S1517-83822009000400010.

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 maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be KM = 54 µmol l-1 and kcat = 190 sec-1 at pH 5.0 and 37°C. The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P5, D-Ins(1,2,5,6)P4, D-Ins(1,2,6)P3, D-Ins(1,2)P2 to finally Ins(2)P.

Palavras-chave : Aspergillus niger; phytate-degrading enzyme; phytate; phytase.

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