氧化多壁碳纳米管-固定化曲霉漆酶杂化材料的制备与表征

H. A.A., Masoud R.A.
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摘要

本文研究了固定化漆酶(Aspergillus sp.)过氧化多壁碳纳米管(ox-MWCNTs)的制备和表征。采用傅里叶红外光谱(FTIR)、热重分析(TGA)、透射电子显微镜(TEM)和动态光散射技术(DLS)对所得材料进行了表征。结果表明,在ox-MWCNTs的情况下,酶固定后的TEM图像显示出更多独立的单个碳束,粒径约为396 nm,而不是直径约为180 nm的意大利面条状管。zeta电位负值(-5 mv)的降低也证明了酶固定化后ox-MWCNT表面的游离羧基减少。此外,TGA固定化后,酶的热稳定性降低。这些结果证实,漆酶可以在ox-MWCNTs的侧壁处反应而不会破坏结构。将固定化漆酶与硝酸银溶液孵育1 h和24 h后,考察了固定化漆酶的生物催化效果。结果表明,室温下硝酸银溶液孵育24 h后,固定化漆酶的生物催化效率相对于游离型有明显提高。另一方面,在50℃和pH 3.0条件下固定化后,酶的稳定性得到改善,而在酸性pH范围内(4 ~ 6),固定化和游离漆酶的活性值没有显著差异。
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Preparation and characterization of oxidized Multi-walled Carbon Nanotubes-Immobilized Aspergillus sp. Laccase Hybrid Materials
This work deals with preparation and characterization of immobilized laccase (Aspergillus sp.) over oxidized multi-walled carbon nanotubes (ox-MWCNTs) via simple mixing technique. The resulting materials were characterized by Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), transmission electron microscope (TEM) and particle size distribution analysis using dynamic light scattering technique (DLS). The results showed that the TEM images exhibited more separate individual carbon bundles with particle size around of 396 nm after enzyme immobilization rather than the spaghetti-like tubes with size about 180 nm in the case of ox-MWCNTs. Also, the lowering in the zeta potential negative value (-5 mv) proved that the free carboxyl groups at ox-MWCNT surface were decreased after enzyme immobilization. Moreover, the thermal stability was decreased after enzyme immobilization using TGA. These results confirmed that the laccase could be reacted at the side walls of the ox-MWCNTs without structure damage. The biocatalytic effect of the immobilized laccase was investigated after its incubation with silver nitrate solution for 1 and 24 h. It can be concluded that the biocatalytic efficiency of the immobilized laccase could be enhanced after its incubation with silver nitrate solution for 24 h at room temperature relative to the free form. On the other hand, the enzyme stability was improved after immobilization up to 50ºC and at pH 3.0, while no remarkable differences on the activity values were observed for immobilized and free laccases at acidic pH range (4-6).
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