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

被引：29

作者：

Suo, Hongbo ^{[1
]}

Li, Moju ^{[1
]}

Liu, Renmin ^{[1
]}

Xu, Lili ^{[1
]}

机构：

[1] Liaocheng Univ, Sch Pharmaceut Sci, Liaocheng 252059, Shandong, Peoples R China

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 2021年 / 206卷

基金：

中国国家自然科学基金;

关键词：

Ionic liquids; Lipase; Magnetic nanoparticles; Polydopamine; Enzyme immobilization; ENZYME; NANOPARTICLES; BIOCATALYSIS; PROTEIN; UREA; PURIFICATION; INSIGHTS; SOLVENT;

D O I：

10.1016/j.colsurfb.2021.111960

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

In this study, imidazolium-based ionic liquid with [tf2N]- 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 PPLMPDA (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.

引用

页数：8

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