Iwaki M, Nozaki M
J Biochem. 1982 May;91(5):1549-53. doi: 10.1093/oxfordjournals.jbchem.a133845.
Metapyrocatechase [catechol : oxygen 2,3-oxidoreductase, EC 1.13.11.2] was immobilized with cyanogen bromide-activated agarose with a coupling yield of 78% of the protein added. The immobilized enzyme showed a specific activity of 77 mumol/min/mg protein, which is about 30% of that of the native enzyme. The immobilization enhanced the stability of the enzyme against inactivation by heat, acid or alkaline pH, and various denaturing agents. However, like the native enzyme, the immobilized enzyme was rapidly inactivated by oxidants such as oxygen or hydrogen peroxide, and the inactivation was completely prevented in the presence of low concentrations of organic solvents. The pH profile for the activity and the substrate specificity were slightly changed by the immobilization.
间苯二酚酶[儿茶酚：氧2,3 -氧化还原酶，EC 1.13.11.2]用溴化氰活化琼脂糖固定化，偶联产率为加入蛋白质的78%。固定化酶的比活性为77 μmol/分钟/毫克蛋白质，约为天然酶的30%。固定化增强了酶对热、酸或碱性pH以及各种变性剂失活的稳定性。然而，与天然酶一样，固定化酶会被氧气或过氧化氢等氧化剂迅速失活，在低浓度有机溶剂存在下可完全防止失活。固定化使活性的pH曲线和底物特异性略有变化。
