Loseva A L, Verbilenko S V
Ukr Biokhim Zh (1978). 1979 Jul-Aug;51(4):345-9.
A complex of Str. griseus proteases was obtained. The proteases were immobilized on Sephadex G-200 and agarose by the bromo-cyanogen method and on the microcrystalline cellulose by means of TiCl3. The enzymic complex immobilized on different carriers possesses the proteolytic activity of a wide specificity. Due to addition to different carriers the activity of certain enzymes producing the complex varies. The immobilized complex is shown to be more stable in the alkaline zone. The immobilized complex is shown to be more stable in the alkaline zone. The temperature optimum of the activity of the immobilized forms is higher than in the initial enzyme and is 70--75 degrees C. Under multiple application of the immobilized forms of the protease complex the preparation obtained on Sephadix G-200 by the bromo-cyanogen method is most stable: it retains 70% of initial activity after 10-repeated applications.
获得了灰色链霉菌蛋白酶复合物。通过溴化氰法将蛋白酶固定在葡聚糖凝胶G - 200和琼脂糖上,并通过TiCl₃将其固定在微晶纤维素上。固定在不同载体上的酶复合物具有广泛特异性的蛋白水解活性。由于添加到不同载体上,产生复合物的某些酶的活性会有所不同。固定化复合物在碱性区域表现出更高的稳定性。固定化复合物在碱性区域表现出更高的稳定性。固定化形式的活性最适温度高于初始酶,为70 - 75摄氏度。在多次应用蛋白酶复合物的固定化形式时,通过溴化氰法在葡聚糖凝胶G - 200上获得的制剂最稳定:在重复应用10次后仍保留70%的初始活性。