Isolation and characterization of extra- and intra-cellular metal proteinases produced in the spawn-running process of Hypsizygus marmoreus

Abstract

Isolation and characterization of extra-(PE-1) and intra-cellular (PE-2) metal proteinases produced during the spawn-running process of Hypsizygus marmoreus were carried out. These enzymes were the most active toward Hammarsten casein at pH 7.0 (PE-1) and pH 6.5-7.5 (PE-2). The molecular weight and pl value of PE-1 were 29,500, 8.8, and those of PE-2 were 21,500, 8,4. Km values against the synthetic peptide substrate Z-Gly-L-Leu.NH2 were 0.9 × 10-3 M (PE- 1) and 1.2 × 10-3 M (PE-2). PE-1 was strongly inhibited by phosphoramidon, whereas PE-2 was weakly inhibited. These enzymes are considered to play an important role in providing nitrogenous substrates during fruit-body formation.