Purification and characterisation of a highly thermostable extracellular protease fromBacillus thermantarcticus, strain M1

@article{Dipasquale2009PurificationAC,
  title={Purification and characterisation of a highly thermostable extracellular protease fromBacillus thermantarcticus, strain M1},
  author={Laura Dipasquale and Valeria Calandrelli and Ida Romano and Barbara Nicolaus and Agata Gambacorta and Licia Lama},
  journal={Annals of Microbiology},
  year={2009},
  volume={58},
  pages={253-259}
}
A high thermostable extracellular protease was purified to homogeneity and characterised fromBacillus thermantarcticus, strain M1. The molecular mass was about 42 kDa. Almost total inhibition of protease by phenyl methyl sulphonylfluoride (PMSF), suggested that the enzyme belonged to the serine protease family. The enzyme was active and stable in a broad range of pH with an optimum at pH 7.0. The protease showed the highest activity at 70°C and was stable for 24 h at 70°C, with an increase of… CONTINUE READING

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