抄録
To investigate the function of proteinases in the fruiting of Basidiomycetes, we purified the neutral proteinase in vegetative mycelium of Lentinus edodes. About 1.6 mg of purified enzyme was obtained from 1.5 kg of mycelium. The purified enzyme was confirmed to be monodispersi ve on disc electrophoresis.
The neutral proteinase was most active around pH 7.5 toward hemoglobin and 7.0 toward casein and was extremely labile with temperature. The enzyme was strongly inhibited by EDTA or Talopeptin (MK-I). The molecular weight and isoelectric point of the enzyme were 45, 000 and pH 5.3, respectively. The enzyme contained no methionine residues. The enzyme hydrolyzed the bonds involving hydrophobic or bulky amino acid residues of oxidized insulin B-chain such as His-Leu (10-11 and 5-6), Leu (17)-Val (18) and Ala (14)-Leu (15).
These characteristics are compared with those of the metal proteinase in the fruit-body of the same fungus, which was purified and characterized at the same time as in vegetative mycelium. We also compare it with proteinases from other microbes.
