Purification and characterization of a thermostable extracellular phytase from Bacillus licheniformis PFBL-03.

@article{Fasimoye2014PurificationAC,
  title={Purification and characterization of a thermostable extracellular phytase from Bacillus licheniformis PFBL-03.},
  author={Feyisola O Fasimoye and Folasade Mayowa Olajuyigbe and Morakinyo D Sanni},
  journal={Preparative biochemistry & biotechnology},
  year={2014},
  volume={44 2},
  pages={
          193-205
        }
}
Extracellular phytase from Bacillus licheniformis PFBL-03 was purified in three steps by using ammonium sulfate precipitation, ion-exchange chromatography on a DEAE Sephadex A-50 column, and gel filtration chromatography on Sephadex G-100. The single protein band on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) suggested that the enzyme was homogeneous. The molecular mass determined from SDS-PAGE was 36 kD. The enzyme yield was 10% while the purification fold was 39. The… CONTINUE READING
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