Purification and characterization of a novel thermostable phytase from the thermophilic Geobacillus sp TF16
Articles > Article ยท 2017
Authors: Emre DOKUZPARMAK, Yakup Sirin, Ummuhan Cakmak, Nagihan Saglam Ertunga
INTERNATIONAL JOURNAL OF FOOD PROPERTIES, Journal Indexed in SCI Expanded, International, 2017, vol 20, pp 1104-1116
DOI: 10.1080/10942912.2016.1203930
Summary
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.