Purification and characterization of a novel thermostable phytase from the thermophilic Geobacillus sp TF16

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Dokuzparmak E., Şirin Y., Cakmak U., Ertunga N.

INTERNATIONAL JOURNAL OF FOOD PROPERTIES, vol.20, no.5, pp.1104-1116, 2017 (SCI-Expanded) identifier identifier


A novel phytase from thermophilic Geobacillus sp. TF16 was purified approximately 5-fold using ammonium sulfate precipitation and ion exchange chromatography, and determined as a single band 106.04 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and optimum pH were found to be 85 degrees C and 4.0, respectively. The enzyme is highly thermostable and V-max and K-m values were calculated as 526.28 U/mg and 1.31 mM, respectively. It was also found that the enzyme exhibited a broad substrate selectivity and resistance toward proteases and effectively hydrolyzed soymilk phytate. These results suggest that this study provides an alternative phytase enzyme with enhanced properties.