Ramachandran K B, Perlmutter D D
Biotechnol Bioeng. 1976 May;18(5):669-84. doi: 10.1002/bit.260180507.
Glucose oxidase from Aspergillus niger was immobilized on nonporous glass beads by covalent bonding and its kinetics were studied in a packed-column recycle reactor. The optimum pH of the immobilized enzyme was the same as that of soluble enzyme; however, immobilized glucose oxidase showed a sharper pH-activity profile than that of the soluble enzyme. The kinetic behavior of immobilized glucose oxidase at optimum pH and 25 degrees C was similar to that of the soluble enzyme, but the immobilized material showed increased temperature sensitivity. Immobilized glucose oxidase showed no loss in activity on storage at 4 degrees C for nearly ten weeks. On continuous use for 60 hr, the immobilized enzyme showed about a 40% loss in activity but no change in the kinetic constant.
通过共价键合将黑曲霉葡萄糖氧化酶固定在无孔玻璃珠上，并在填充柱循环反应器中研究其动力学。固定化酶的最适pH与可溶性酶相同；然而，固定化葡萄糖氧化酶的pH活性曲线比可溶性酶更陡。在最适pH和25℃下，固定化葡萄糖氧化酶的动力学行为与可溶性酶相似，但固定化材料表现出更高的温度敏感性。固定化葡萄糖氧化酶在4℃储存近十周后活性没有损失。连续使用60小时后，固定化酶的活性损失约40%，但动力学常数没有变化。
