Purification and Characterization of an Aminopeptidase from the Edible Basidiomycete Grifola frondosa
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概要
- 論文の詳細を見る
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 27kDa and 30kDa 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.
- 社団法人日本農芸化学会の論文
- 2001-02-23
著者
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Hayashi Kiyoshi
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries
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Nishiwaki Toshikazu
Food Research Center Niigata Agricultural Research Institute
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Nishiwaki Toshikazu
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries
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Hayashi Kiyoshi
National Food Research Institute
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