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Provedor de dados:  BJM
País:  Brazil
Título:  Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9
Autores:  Greiner,Ralf
Silva,Lucineia Gomes da
Couri,Sonia
Data:  2009-12-01
Ano:  2009
Palavras-chave:  Aspergillus niger
Phytate-degrading enzyme
Phytate
Phytase
Resumo:  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 K M = 54 µmol l-1 and k cat = 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.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822009000400010
Editor:  Sociedade Brasileira de Microbiologia
Relação:  10.1590/S1517-83822009000400010
Formato:  text/html
Fonte:  Brazilian Journal of Microbiology v.40 n.4 2009
Direitos:  info:eu-repo/semantics/openAccess
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