顺磁性纳米颗粒固定化真菌过氧化物酶用于合成染料脱色

K. Omeje, Chinonso Magbo, E. Ossai, J. Ozioko, B. O. Ezema, N. Nnolim, S. Eze
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引用次数: 1

摘要

黄曲霉KIGC以香蕉皮为唯一碳源,发酵第11天产生过氧化物酶。纯化得到8.86层,回收率为49.72%。将纯化的过氧化物酶固定在磁性纳米颗粒上,用DLS、DSC、XRD、FTIR和SEM对其进行了表征。结果表明,制备的纳米颗粒充足,酶固定化效果良好。游离过氧化物酶和固定化过氧化物酶的最适温度分别为75℃和70℃,游离过氧化物酶的最适pH分别为5.0和9.0,固定化过氧化物酶的最适pH分别为6.5和9.0。以愈创木酚为底物,固定化过氧化物酶的Km为0.075mM,催化效率为90.66 Mol/S-1。固定化过氧化物酶对合成染料的脱色能力增强。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Immobilization of Fungal Peroxidase on Paramagnetic Nanoparticles for Synthetic Dye Decolorization
: Peroxidase was produced by Aspergillus flavus KIGC on 11 th day of fermentation when grown on banana peel as the sole carbon source. It was purified to 8.86 folds with percentage recovery of 49.72%. The purified peroxidase was immobilized on magnetic nanoparticle and character-ized using DLS, DSC, XRD, FTIR and SEM analyses. The results suggest adequate nanoparticle for-mulation and effective enzyme immobilization. Optimal temperatures for free and immobilized peroxidase were 75 and 70 °C, respectively, optimum pH of 5.0 and 9.0 were obtained for free enzyme and 6.5 and 9.0 for immobilized peroxidase, respectively. The Km of 0.075mM and catalytic efficiency of 90.66 Mol/S-1 were achieved by the immobilized peroxidase on guaiacol as substrate. The immobilized peroxidase exhibited enhanced synthetic dyes decolorization ability.
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