Voĭnarskiĭ I N, Iarovenko V L
Prikl Biokhim Mikrobiol. 1975 Sep-Oct;11(5):717-24.
The enzymic preparation isolated by ethanol precipitation from the aqueous extract of the surface culture of Aspergillus terricola was purified on biogel P-10, fractionated on SE-Sephadex. As a result, 10 fractions of acid proteinases that differed in pH optima and activity were obtained. After purification specific activity of some fractions per 1 mg protein increased 24-32-fold. The temperature optimum of the enzymes was at 50 degrees C and pH optimum at 2.5--2.8.
从土曲霉表面培养物水提取物中通过乙醇沉淀分离得到的酶制剂，在生物凝胶P - 10上进行纯化，并在SE - 葡聚糖凝胶上进行分级分离。结果得到了10个在最适pH值和活性方面存在差异的酸性蛋白酶组分。纯化后，某些组分每1毫克蛋白质的比活性提高了24 - 32倍。这些酶的最适温度为50℃，最适pH值为2.5 - 2.8。
