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

ABSTRACT

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°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.

KEYWORDS:

• Characterization
• Geobacillus
• Phytase
• Purification, Thermostable

Acknowledgments

The authors would like to thank Assistant Professor Dr. Kadriye Inan Bektas for providing the bacterium strain.

Funding

This work was supported by TUBITAK (Project number is 214Z190).

Additional information

Funding

This work was supported by TUBITAK (Project number is 214Z190).