%0 Journal Article
%T Purification and properties of a phytate-degrading enzyme produced by Enterobacter sakazakii ASUIA279
%A Abd-ElAziem Farouk
%A Ralf Greiner
%A Anis Shobirin Meor Hussin
%J Journal of Biotechnology and Biodiversity
%D 2012
%I Federal University of Tocantins
%X An extracellular phytate-degrading enzyme produced by Enterobacter sakazakii ASUIA279 was purified to homogeneity using FPLC anion exchange chromatography and gel filtration. The enzyme was purified about 66-fold with a recovery of 27%. Its molecular mass was estimated to be 43 kDa by SDS-PAGE. The Michaelis constant (KM) and turnover number (kcat ) for sodium phytate at pH 5.0 and 50¡ãC were calculated from the Lineweaver-Burk plot to be 760 ¦ÌM and 4.14s-1, respectively. The enzyme showed narrow substrate specificity and not phytate, but GTP was dephosphorylated with the highest relative rate of hydrolysis. However, according to the kcat/KM values, phytate was concluded to be the in vivo substrate of the enzyme. Optimal activity was determined at pH 4.5 and 45-55¡ãC. The enzyme was strongly inhibited by Fe3+, Cu2+, Zn2+, molybdate, vanadate, fluoride and phosphate (1 mM).
%K Enterobacter sakazakii
%K phytate-degrading enzyme
%K phytate
%K purification
%U http://revista.uft.edu.br/index.php/JBB/article/view/173/115