固定在伴刀豆球蛋白A-琼脂糖上的核糖核酸酶T2的制备及性质
Preparation and properties of RNase T2 immobilized on concanavalin A-sepharose.
作者信息
Reddy L G, Shankar V
机构信息
Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
出版信息
Appl Biochem Biotechnol. 1989 Dec;22(3):237-46. doi: 10.1007/BF02921759.
Partially purified RNase T2 (EC 2.7.7.17) from Aspergillus oryzae was bound through its carbohydrate moiety to Concanavalin A-Sepharose. The retention of activity was high, ranging from 70% at low enzyme load to approximately 9% at high enzyme load. Though there was no change in the pH and temperature optima, the pH stability and the Km decreased after immobilization. Compared to the soluble enzyme, the immobilized RNase T2 showed enhanced temperature stability and more resistance to metal ions. Both soluble and immobilized enzymes were stable to 8 M urea. On repeated use, the bound enzyme retained more than 60% of its initial activity after six cycles.
从米曲霉中部分纯化得到的核糖核酸酶T2（EC 2.7.7.17）通过其碳水化合物部分与伴刀豆球蛋白A-琼脂糖结合。活性保留率较高，在低酶负载量时为70%，在高酶负载量时约为9%。虽然最适pH和温度没有变化，但固定化后pH稳定性和米氏常数降低。与可溶性酶相比，固定化核糖核酸酶T2表现出更高的温度稳定性和对金属离子更强的耐受性。可溶性酶和固定化酶在8 M尿素中均稳定。重复使用时，结合酶在六个循环后仍保留其初始活性的60%以上。
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