Institute of Chemical Technology and Engineering, Faculty of Chemical Technology, Poznan University of Technology, Berdychowo 4, PL-60965, Poznan, Poland.
Faculty of Materials Science and Engineering, Warsaw University of Technology, Wołoska 141, PL-02507, Warsaw, Poland.
Environ Res. 2020 May;184:109332. doi: 10.1016/j.envres.2020.109332. Epub 2020 Mar 2.
Novel electrospun poly(methyl methacrylate)/polyaniline electrospun fibres were produced, characterised, modified, and used as a support for laccase immobilisation by two methods: adsorption and covalent binding. Effective deposition of laccase by both methods was confirmed by FTIR and CLSM results. Nevertheless, the main objective of the study was to select the most favourable immobilisation conditions and prepare heterogeneous biocatalysts with the best possible catalytic properties. The highest relative activity of enzymes immobilised by adsorption and covalent binding were obtained after 1 h of immobilisation using laccase solution at a concentration of 1 mg/mL, at pH 5 and 25 °C. It was found that the immobilised enzymes, which were present in amounts of 110 mg/g and 185 mg/g for systems with adsorbed and covalently bonded laccase respectively, exhibited slightly lower substrate affinity, and in consequence also a lower maximum reaction rate, than the free enzyme. The stability of laccase improved significantly upon immobilisation: both heterogeneous biocatalysts retained over 80% relative activity even after 10 repeated catalytic cycles and 30 days of storage. The obtained systems were used for decolourisation of Remazol Brilliant Blue R dye from a model aqueous solution, resulting in removal efficiencies of 87% and 58% using adsorbed and covalently bonded laccase, respectively. The described approach to the removal of textile dye from model solution is significant for the sustainable and environmentally friendly decolourisation of various compounds from wastewater.
新型聚甲基丙烯酸甲酯/聚苯胺电纺纤维被制备、表征、修饰，并通过两种方法（吸附和共价结合）用作固定化漆酶的载体：吸附和共价结合。FTIR 和 CLSM 结果证实了两种方法都能有效地固定化漆酶。然而，本研究的主要目的是选择最有利的固定化条件，并制备具有最佳催化性能的异相生物催化剂。使用 1 mg/mL 浓度的漆酶溶液，在 pH 5 和 25°C 下，通过吸附和共价结合固定化 1 小时，可获得相对酶活性最高的固定化酶。发现固定化酶的酶量分别为 110 mg/g 和 185 mg/g，其底物亲和力略低，因此最大反应速率也低于游离酶。固定化后，漆酶的稳定性显著提高：两种异相生物催化剂在 10 次重复催化循环和 30 天储存后，仍保留超过 80%的相对活性。所得体系用于从模型水溶液中去除 Remazol Brilliant Blue R 染料，吸附和共价结合固定化漆酶的去除效率分别为 87%和 58%。从模型溶液中去除纺织染料的这种方法对于可持续和环保地去除废水中的各种化合物具有重要意义。
