Purification and Properties of Neutral Proteinase I from Aspergillus oryzae
Purification and Properties of Neutral Proteinase I from Aspergillus oryzae
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米曲霉中性蛋白酶I的纯化及性质
DOI：
10.1271/bbb1961.37.2695
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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
中性蛋白酶I（DEAE-纤维素层析中的第一个峰）通过DEAE-纤维素层析和SephadexG-100凝胶过滤从Amberlite IRC-50吸附级分中纯化。它显示了牛奶酪蛋白的最适pH值为7.0。发现该酶在pH值5.5至12.0范围内稳定。凝胶过滤法测得该酶的分子量约为41，000。该酶既没有氨肽酶活性，也没有羧肽酶活性，但能降解苄氧羰基甘氨酰苯丙氨酸酰胺、聚L-赖氨酸和聚L，a-谷氨酸。该酶能被乙二胺四乙酸抑制，但不被二异丙基氟磷酸和马铃薯抑制剂抑制。
Neutral proteinase I (the first peak in DEAE-cellulose chromatogrraphy) was purified from the Amberlite IRC-50 adsorbed fraction by chromatography on DEAE-cellulose and gel filtration through Sephadex G-100. It shows an optimum pH of 7.0 for milk casein. The enzyme was found to be stable in the pH range of 5.5 to 12.0. The molecular weight of the enzyme was estimated to be about 41, 000 by gel filtration. The enzyme had neither aminopeptidase nor carboxypeptidase activity, but degraded carbobenzoxy-glycyl-phenylalanine amide, poly-L-lysine and poly-L, a-glutamic acid. The enzyme was inhibited by ethylenediaminetetraacetate, but not inhibited by diisopropylphosphorofluoridate and potato inhibitor.