Purification and characterization of an aminopeptidase from the edible basidiomycete Grifola frondosa.

@article{Nishiwaki2001PurificationAC,
  title={Purification and characterization of an aminopeptidase from the edible basidiomycete Grifola frondosa.},
  author={Toshikazu Nishiwaki and Kunihiko Hayashi},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2001},
  volume={65 2},
  pages={424-7}
}
An aminopeptidase was purified 178-fold from an extract of Grifola frondosa by ammonium sulfate precipitation and a series of column chromatographies on phenyl-Toyopearl, Sephadex G-25, and Mono-Q. The molecular mass of the enzyme was estimated to be 27 kDa and 30 kDa by gel filtration and SDS-PAGE, respectively. The enzyme had an optimum pH of 8.5 and was stable between pH 6.0 and pH 10.5, and it also had a high level of heat stability. The enzyme was inactivated by EDTA and o-phenanthroline… CONTINUE READING