A heterogeneous bead-shaped biocatalyst was prepared by assembling co-immobilization of encapsulating mediator 2,2′-Azino-bis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) into the functionalized calcium alginate composite beads by grafting glycidyl methacrylate and dopamine and then immobilizing laccase covalently onto beads. The enzyme-catalyzed degradation for acridine in water was systematically studied for the first time, and it was found that the co-immobilized laccase-mediator system has excellent capability to degrade acridine in water. Treating 30 mg/L acridine aqueous solution for 8 h with the biocatalyst, the degradation rate of acridine reached 100 %. In contrast, the degradation of acridine by free laccase under the same treatment conditions was low and difficult to observe. Its outstanding catalytic activity could be attributed to the effective assembling co-immobilization of laccase and the mediator so that the catalytic activity of the enzyme and the synergistic promoting action of the mediator have been given full play in the process of acridine degradation. The beaded biocatalyst about 3 mm in diameter could be easily recovered and reused several times without obvious deterioration in catalytic activity. Furthermore, according to the test results of electron paramagnetic resonance and the identified intermediates, the possible biocatalytic mechanism and reaction pathways for acridine degradation have been proposed.

通过将甲基丙烯酸缩水甘油酯和多巴胺接枝，将包封介质2,2'-叠氮-双-（3-乙基苯并噻唑啉-6-磺酸盐）（ABTS）共固定到官能化的藻酸钙复合材料珠中，制备了非均相的珠状生物催化剂然后将漆酶共价固定在珠子上。首次系统地研究了酶催化的水中degradation啶的降解，发现共固定的漆酶-介体体系具有优异的降解水中a啶的能力。用生物催化剂处理30 mg / LL啶水溶液8 h，the啶的降解率达到100％。相反，在相同的处理条件下，游离漆酶对of啶的降解较低，难以观察到。其优异的催化活性可以归因于漆酶和介体的有效组装共固定化，从而在of啶的降解过程中充分发挥了酶的催化活性和介导的协同促进作用。直径约3 mm的珠状生物催化剂可以轻松回收并重复使用数次，而催化活性不会明显降低。此外，根据电子顺磁共振和鉴定出的中间体的测试结果，提出了可能的bio啶降解的生物催化机理和反应途径。