Deniakina E K, Nekliudov A D, Loginova T A, Krest'ianova I A, Bartoshevich Iu E
Prikl Biokhim Mikrobiol. 1985 Mar-Apr;21(2):177-83.
A heterogeneous multienzyme preparation with the peptidase activity, isolated from the cells of Pseudomonadacea bacteria, was immobilized on alumina. The specific activity of the immobilized enzyme complex is not a simple function of the bound protein quantity, but depends on immobilization conditions. An additional glutaraldehyde treatment results in higher thermostability of the immobilized enzyme preparation. The substrate specificity of the preparation retains after immobilization, and it becomes less sensitive to pH changes.
从假单胞菌科细菌细胞中分离出的具有肽酶活性的多酶复合体被固定在氧化铝上。固定化酶复合物的比活性不是结合蛋白量的简单函数,而是取决于固定化条件。额外的戊二醛处理可提高固定化酶制剂的热稳定性。固定化后该制剂的底物特异性得以保留,并且对pH变化的敏感性降低。