Corticium rolfsiiの酸性proteinase
Year: 1981
Type: article
Abstract: On the basis of screening Corticium species, acid proteinase was found to be produced by all 13 strains used. Corticium rolfsii IFO 4878 was selected for the enzymatic study and cultured in a medium containing defatted soybean powder. Acid proteinase was partially purified about 68-fold from the culture fluid by a combination of various column chromatography. The isoelectric point lied at pH 4.33 and the molecular weight was estimated to be 27,500. The enzymatic activity was found to be maximum at pH 2.5 toward milk casein and at 2.0 toward hemoglobin-HCl. The enzyme was stable between pH 1.0 and 5.0. At pH 1.0, the enzyme lost less than 10% of its activity during a 72-hr period at 4℃. The enzymatic activity was inhibited by pepstatin, 1,2-epoxy-3-(p-nitrophenoxy) propane, CN-and Hg2+, but stimulated by Mn2+. The enzyme had an optimal pH for milk-clotting activity between 5.3 and 5.5. The partial purified acid proteinase was demonstrated by its ability to hydrolyze various native proteins.
Language: Japanese
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W7145420044