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Purification and Properties of Alkaline Proteinase from Aspergillus oryzae
Authors:Tadanobu Nakadai  Seiichi Nasuno  Nobuyoshi Iguchi
Affiliation:Noda Institute for Scientific Research, Noda-shi, Chiba-ken
Abstract:
Alkaline proteinase was purified from culture extract of a strain of Aspergillus oryzae. The process consists of the Amberlite IRC-50 adsorption, column chromatography on DEAE-cellulose and CM-cellulose and Sephadex G-100 gel filtration. The molecular weight of the enzyme was estimated to be about 23,000 by a gel filtration method. Alkaline proteinase showed neither carboxypeptidase activity nor aminopeptidase activity, but degraded 10101010 poly-l,α-glutamic acid, poly-l-lysine, 10101010 and 10101010. The enzyme was completely inhibited by diisopropylphos-phorofluoridate (10?2 m) or potato inhibitor (250 μg/ml).
Keywords:
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