Partial purification, characterization and wheat bran degradation studies of a new phytase from the Bacillus megaterium EBD 9-1 strain

Objective: The present study was designed to report the bacterial identification and characterization of a new phytase enzyme from a Bacillus sp. strain isolated from soil. Methods: Bacillus sp. strain was identified based on 16S rRNA analysis. The phytase was partially purified through ammonium sulfate precipitation and Sephadex G100 gel filtration steps, and characterized for its activity and stability. Results: The new isolate EBD 9-1 showed 100% sequence identity with Bacillus megaterium. The partially purified enzyme had the maximum activity at pH 7.0 and 60 degrees C. The activity of the enzyme was stimulated in the presence of Ca+2, V-max and K-m for enzyme were found to be 333 U/mL and 2 mM, respectively. The estimated molecular weight of enzyme was 45 kDa. The storage stability of phytase was 93% of the initial activity after 6 months at 4 degrees C and -20 degrees C. This study represents the partial purification, characterization and wheat bran degradation studies for B. megaterium phytase. Conclusion: Consequently, due to the characteristics such as significant stability at higher temperatures, alkaline pH and storage of the novel phytase enzyme produced by B. megaterium EBD 9-1, the enzyme may be suitable for supplementing animal feeds to improve the availability of phosphorus from phytates.