Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16

@article{Kobayashi2004PurificationAP,
  title={Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16},
  author={T. Kobayashi and Yoshihiro Hakamada and S Adachi and Jun Hitomi and Tadashi Yoshimatsu and Kenzo Koike and Shuji Kawai and Susumu Ito},
  journal={Applied Microbiology and Biotechnology},
  year={2004},
  volume={43},
  pages={473-481}
}
Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala-Gln-Ser-Val-Pro-Trp-Gly-Ile-Ser-Arg-Val-Gln-Ala-Pro-Ala-Ala-His-Asn-Arg-Gly-Leu-Thr-Gly. The molecular mass of the protease was 28 kDa, and its isoelectric… 

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