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Purification and properties of a phytate-degrading enzyme produced by Enterobacter sakazakii ASUIA279.


Citation

Farouk, Abd-ElAziem and Greiner, Ralf and Meor Hussin, Anis Shobirin (2012) Purification and properties of a phytate-degrading enzyme produced by Enterobacter sakazakii ASUIA279. Journal of Biotechnology and Biodiversity , 3 (1). pp. 1-9. ISSN 2179-4804

Abstract

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°C were calculated from the Lineweaver-Burk plot to be 760 µM 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°C. The enzyme was strongly inhibited by Fe3+, Cu2+, Zn2+, molybdate, vanadate, fluoride and phosphate (1 mM).


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Official URL: http://www.uft.edu.br/

Additional Metadata

Item Type: Article
Divisions: Faculty of Food Science and Technology
Publisher: Federal University of Tocantins
Keywords: Enterobacter sakazakii; Phytate-degrading enzyme; Phytate; Purification.
Depositing User: Nur Farahin Ramli
Date Deposited: 09 Oct 2013 01:57
Last Modified: 18 Sep 2015 08:04
URI: http://psasir.upm.edu.my/id/eprint/24200
Statistic Details: View Download Statistic

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