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  • Title: Purification and characterization of an aminopeptidase from the edible basidiomycete Grifola frondosa.
    Author: Nishiwaki T, Hayashi K.
    Journal: Biosci Biotechnol Biochem; 2001 Feb; 65(2):424-7. PubMed ID: 11302180.
    Abstract:
    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, and it was also strongly inhibited by bestatin, but no inhibitory effect of DFP was observed. The enzyme preferentially hydrolyzed peptides containing hydrophobic residues in the N-terminal position.
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