ABSTRACT
The development of immobilized enzymes with high activity and stability is critical. Metal-organic frameworks (MOFs) have attracted much academic and industrial interest in the field of enzyme immobilization due to their unique properties. In this study, the amino-functionalized ionic liquid (NIL)-modified metal-organic framework (UiO-66-NH2) was prepared to immobilize Candida rugosa lipase (CRL), using dialdehyde starch (DAS) as the cross-linker. The results of the Fourier transform infrared (FT-IR) spectra, X-ray powder diffraction (XRD), and scanning electronic microscopy (SEM) confirmed that the NIL was successfully grafted to UiO-66-NH2. The CRL immobilized on NIL-modified UiO-66-NH2 (UiO-66-NH2-NIL-DAS@CRL) exhibited satisfactory activity recovery (79.33%), stability, reusability, and excellent organic solvent tolerance. The research results indicated that ionic liquid-modified UiO-66-NH2 had practical potential for application in enzyme immobilization.
Subject(s)
Enzymes, Immobilized , Ionic Liquids , Lipase , Metal-Organic Frameworks , Lipase/chemistry , Lipase/metabolism , Ionic Liquids/chemistry , Enzymes, Immobilized/chemistry , Metal-Organic Frameworks/chemistry , Enzyme Stability , Spectroscopy, Fourier Transform Infrared , X-Ray Diffraction , Starch/chemistry , Starch/analogs & derivatives , Saccharomycetales/enzymology , Phthalic AcidsABSTRACT
The bio-enzyme degradation technology is a promising approach to sustainably remove pollution in the water and laccase is one of the most widely used enzymes in this area. Nevertheless, the further industrial application of laccase is limited by low stability, short service, low reusability and high price. The immobilization technology can significantly improve the stability and reusability of enzymes and thus promoting their industrial applications. Nanocomposite materials have been developed and applied in the efficient immobilization of laccase due to their superior physical, chemical, and biological performance. This paper presents a comprehensive review of various nanocomposite immobilization methods for laccase and the consequent changes in enzymatic properties post-immobilization. Additionally, a comprehensive analysis is conducted on the factors that impact laccase immobilization and its water removal efficiency. Furthermore, this review examines the effectiveness of common contaminants' removal mechanisms while summarizing and discussing issues related to laccase immobilization on nanocomposite carriers. This review aims to provide valuable guidance for enhancing laccase immobilization efficiency and enzymatic water pollutant removal.
