Ananichev A V, Ulezlo I V, Rezuikov A A, Bezborodov A M, Egorov A M
Biokhimiia. 1978 Jul;43(7):1294-302.
Glucose-isomerizing enzyme was isolated from the culture of Actinomyces olivocinereus. It was purified by the chromatography on DEAE-cellulose. The samples of glucose-isomerasing enzyme are homogeneous according to the results of analytical electrophoresis and ultracentrifugation. Glucose-isomerase is more stable than soluble one. The pH-optima of soluble and immobilized enzymes are 8.5 and 7.5, respectively. The temperature optimum of immobilized enzyme, Km, V, and activation energy do not change during immobilization. The immobilized sample has 58% activity of soluble enzyme.
葡萄糖异构酶是从橄榄灰链霉菌培养物中分离得到的。通过DEAE - 纤维素柱层析进行纯化。根据分析电泳和超速离心结果,葡萄糖异构酶样品是均一的。固定化葡萄糖异构酶比可溶性葡萄糖异构酶更稳定。可溶性酶和固定化酶的最适pH分别为8.5和7.5。固定化酶的最适温度、米氏常数(Km)、最大反应速度(V)和活化能在固定化过程中不变。固定化样品具有可溶性酶58%的活性。