Purification and some properties of an isoform of metal proteinases from Hypsizygus marmoreus grown on sawdust culture

Purification and some properties of an isoform of metal proteinase from Hypsizygus marmoreus are described. This enzyme was purified 711-fold with 5.44% recovery. The molecular weight and pl value were 41,500 and pH 7.7, respectively. The highest activity was observed against milk casein as the subs...

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Veröffentlicht in:Mycoscience 1998-12, Vol.39 (4), p.471-474
Hauptverfasser: Terashita, Takao, Nakaie, Yoko, Yoshikawa, Kentaro, Shishiyama, Jiko
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Sprache:eng
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Zusammenfassung:Purification and some properties of an isoform of metal proteinase from Hypsizygus marmoreus are described. This enzyme was purified 711-fold with 5.44% recovery. The molecular weight and pl value were 41,500 and pH 7.7, respectively. The highest activity was observed against milk casein as the substrate. This enzyme was strongly inhibited by metal proteinase inhibitors such as phosphoramidon, EDTA, and o-phenanthroline.
ISSN:1340-3540
1618-2545
DOI:10.1007/BF02460908