School of Biological and Chemical Engineering, Anhui Polytechnic University, Wuhu, 241000, China; Anhui Laboratory of Functional Coordinated Complexes for Materials Chemistry and Application, Anhui Polytechnic University, Wuhu, 241000, China.
School of Biological and Chemical Engineering, Anhui Polytechnic University, Wuhu, 241000, China; Anhui Laboratory of Functional Coordinated Complexes for Materials Chemistry and Application, Anhui Polytechnic University, Wuhu, 241000, China.
J Hazard Mater. 2020 Nov 15;399:123088. doi: 10.1016/j.jhazmat.2020.123088. Epub 2020 Jun 4.
An effective strategy for enhancement of catalytic activity and stability of immobilized laccase via metal affinity adsorption on FeO@C-Cu nanoparticles was developed, which involved the fabrication of hydroxyl and carboxyl functionalized FeO@C nanoparticles via a simple hydrothermal process and the subsequent chelation with Cu for the immobilization of laccase under a mild condition. Our results revealed that the FeO@C-Cu nanoparticles possess a high loading amount of bovine serum albumin (BSA, 436 mg/g support) and laccase activity recovery of 82.3 % after immobilization. Laccase activity assays indicated that thermal and pH stabilities, and resistances to organic solvents and metal ions of the immobilized laccase were relatively higher than those of the free enzyme. The immobilized laccase maintained more than 61 % of its original activity after 10 consecutive reuses. Most importantly, the immobilized laccase possessed excellent degradation of diverse synthetic dyes. The degradation rates of malachite green (MG), brilliant green (BG), crystal violet (CV), azophloxine, Procion red MX-5B, and reactive blue 19 (RB19) was approximately 99, 93, 79, 88, 75 and 81 (%) in the first cycle. Even after 10 consecutive reuses, the removal efficiencies of the six dyes were found to be 94, 80, 71, 78, 60, and 65 (%), respectively.
通过金属亲和吸附在 FeO@C-Cu 纳米粒子上，开发了一种有效提高固定化漆酶催化活性和稳定性的策略，该策略涉及通过简单的水热法制备羟基和羧基功能化的 FeO@C 纳米粒子，然后在温和条件下与 Cu 螯合固定化漆酶。我们的结果表明，FeO@C-Cu 纳米粒子具有较高的牛血清白蛋白（BSA，436mg/g 载体）负载量和固定化漆酶的 82.3%的酶活回收率。漆酶活性测定表明，固定化漆酶的热稳定性、pH 稳定性、有机溶剂和金属离子抗性均高于游离酶。固定化漆酶在连续重复使用 10 次后，仍保持其原始活性的 61%以上。最重要的是，固定化漆酶对多种合成染料具有优异的降解性能。在第一个循环中，孔雀石绿（MG）、亮绿（BG）、结晶紫（CV）、偶氮荧光黄、普施安红 MX-5B 和活性蓝 19（RB19）的降解率分别约为 99%、93%、79%、88%、75%和 81%。即使在连续重复使用 10 次后，六种染料的去除效率仍分别为 94%、80%、71%、78%、60%和 65%。
