Purification and Properties of Alkaline Proteinase from Aspergillus oryzae
Purification and Properties of Alkaline Proteinase from Aspergillus oryzae
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米曲霉碱性蛋白酶的纯化及性质
DOI：
10.1271/bbb1961.37.2685
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发表时间：
1973
期刊：
影响因子：
--
通讯作者：
N. Iguchi
中科院分区：
文献类型：
--
作者：
T. Nakadai;S. Nasuno;N. Iguchi
从一株米曲霉的培养液中纯化出碱性蛋白酶。该工艺包括Amberlite IRC-50吸附，deae -纤维素和cm -纤维素的柱层析和Sephadex G-100凝胶过滤。通过凝胶过滤法估计酶的分子量约为23000。碱性蛋白酶既没有羧肽酶活性，也没有氨基肽酶活性，但能降解10101010聚l、α-谷氨酸、聚赖氨酸、10101010和10101010。氟化二异丙基磷（10−2 m）或马铃薯抑制剂（250 μg/ml）均能完全抑制该酶。
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).