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增强固定在离子液体修饰的磁性聚多巴胺上的脂肪酶的生物催化性能。

Enhancing bio-catalytic performance of lipase immobilized on ionic liquids modified magnetic polydopamine.

机构信息

School of Pharmaceutical Sciences, Liaocheng University, Liaocheng, Shandong, 252059, China.

School of Pharmaceutical Sciences, Liaocheng University, Liaocheng, Shandong, 252059, China.

出版信息

Colloids Surf B Biointerfaces. 2021 Oct;206:111960. doi: 10.1016/j.colsurfb.2021.111960. Epub 2021 Jun 30.

Abstract

In this study, imidazolium-based ionic liquid with [tfN] as the anion was successfully grafted to magnetic polydopamine nanoparticles (MPDA). The prepared materials were well characterized and used as supports for lipase immobilization. The immobilized lipase (PPL-ILs-MPDA) exhibited excellent activity and stability. The specific activity of PPL-ILs-MPDA was 2.15 and 1.49 folds higher than that of free PPL and PPL-MPDA. In addition, after 10 rounds of reuse, the residual activity of PPL-ILs-MPDA was 86.2 % higher than that of PPL-MPDA (75.4 %). Furthermore, the kinetic assay indicated that the affinity between PPL-ILs-MPDA and substrate had increased. Analysis of the secondary structure using circular dichroism was used to explain the mechanism underlying the improvement in the performance of PPL-ILs-MPDA. In addition, the immobilized lipase can be easily separated from the reaction system with a magnet. The observations regarding the development of new supports for lipase immobilization may provide new ideas regarding further studies in this field.

摘要

在这项研究中,成功地将[tfN]作为阴离子的咪唑鎓基离子液体接枝到磁性聚多巴胺纳米粒子(MPDA)上。制备的材料得到了很好的表征,并用作脂肪酶固定化的载体。固定化脂肪酶(PPL-ILs-MPDA)表现出优异的活性和稳定性。PPL-ILs-MPDA 的比活度分别是游离 PPL 和 PPL-MPDA 的 2.15 倍和 1.49 倍。此外,经过 10 次重复使用后,PPL-ILs-MPDA 的剩余活性比 PPL-MPDA(75.4%)高 86.2%。此外,动力学分析表明,PPL-ILs-MPDA 与底物之间的亲和力增加。使用圆二色性分析二级结构,解释了 PPL-ILs-MPDA 性能提高的机制。此外,固定化脂肪酶可以用磁铁从反应体系中轻易分离。这些关于新型脂肪酶固定化载体开发的观察结果可能为该领域的进一步研究提供新的思路。

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