Immobilized D-amino acid oxidase.
Immobilized D-amino acid oxidase.
复制标题
固定化D-氨基酸氧化酶。
DOI：
10.1016/0005-2744(78)90004-9
复制
发表时间：
1978
期刊：
影响因子：
--
通讯作者：
K. Yagi
中科院分区：
文献类型：
--
作者：
M. Naoi;K. Yagi
1. D-氨基酸氧化酶（D-氨基酸：氧氧化还原酶（脱氨基），EC 1.4。3.3)脱辅基酶、全酶和酶-苯甲酸盐复合物固定在氨烷基或羧烷基琼脂糖或溴化氰活化的琼脂糖上时具有活性和稳定性。固定化酶-苯甲酸盐复合物可转化为全酶和脱辅基酶而不从琼脂糖中释放出来。2.固定化酶的表观米氏常数和底物特异性与游离酶相似。反应的最适pH值从游离酶的最适pH值向酸性移动1.0-2.0个pH单位。3.随着“间隔基”的亚甲基数目从3增加到5，固定化酶的分子活性增加，而表观Miachaelis常数降低。
1. D-Amino acid oxidase (D-amino acid: oxygen oxidoreductase (deaminating), EC 1.4. 3.3) apoenzyme, holoenzyme and the enzyme-benzoate complex were active and stable when immobilized to aminoalkyl or carboxyalkyl agarose, or to cyanogen bromide-activated agarose. The immobilized enzyme-benzoate complex could be converted into the holo-and apoenzyme without being liberated from the agarose. 2. The apparent Michaelis constant and substrate specificity of the immobilized enzyme were similar to those of the free enzyme. The optimum pH of the reaction was shifted towards acidic side by 1.0-2.0 pH units from that of the free enzyme. 3. With increasing number of methylene groups of the'spacer'from 3 to 5, molecular activity of the immobilized enzyme increased, while the apparent Miachaelis constant decreased.