Fabrication of a magnetic nanoparticle embedded NH₂-MIL-88B MOF hybrid for highly efficient covalent immobilization of lipase

Abstract

Metal-organic frameworks (MOFs), a class of porous hybrid materials composed of metal ions and organic ligands, have been studied for a variety of applications. In this work, for the first time, magnetic MOFs are developed for lipase immobilization. A general one-step in situ hydrothermal route is developed for the construction of MOFs encapsulating superparamagnetic Fe 3 O 4 nanoparticles. The integration of Fe 3 O 4 nanoparticles into MOFs exhibit many interesting inherent properties including porous nature, easy functionalization as well as strong superparamagnetism. Here Candida Rugosa Lipase (CRL) is covalently attached to amino-rich magnetic MOFs. The resulting magnetic MOFs are characterized by means of field emission scanning electron microscopy (FESEM), Fourier transform infrared spectroscopy (FT-IR), thermogravimetric analysis (TGA) and vibrating sample magnetometer (VSM). Then the enzymatic activities of the immobilized CRL are compared with free CRL. The immobilized CRL presented wider pH tolerance and excellent thermal stability than free CRL. The Michaelis-Menten kinetic constant (K m ) and maximum reaction velocity (V max ) for both free and immobilized lipase are investigated. The loading amount of CRL on magnetic MOFs was 280 mg/g support and the immobilized CRL was efficiently recycled up to nine cycles.

Fast Immobilization of Human Carbonic Anhydrase II on Ni-Based Metal-Organic Framework Nanorods with High Catalytic Performance

“…Since MOF materials are considered to be potent supporting matrices for enzyme immobilization, many kinds of commodity enzymes were immobilized successfully [25][26][27][28]. However, other researchers have spent their energy on the design of Zn 2+ , Cu 2+ or Fe 3+ -based MOFs for enzyme immobilization [29][30][31]. Inspired by the specific affinity between Ni 2+ and histidine-tags [32], we focus on utilizing Ni-based MOFs to achieve one-pot immobilization of histidine-tagged enzymes.…”

Magnetically responsive horseradish peroxidase@ZIF-8 for biocatalysis

“…24 Alternatively, enzymes were immobilised on the surface of pre-synthesized magnetic MOF core-shell systems. 25,26 Thus, the available methods either require the use of compatibilizing agents or multi-step procedures.…”

“…The one-pot synthesis was conducted at room temperature in water, overcoming previously reported limitations, such as multistep synthesis, 25 need for polymeric additives, organic solvents, 23,24 or surface functionalization processes. 26 HRP/MNP@ZIF-8 was characterized by SEM, XRD, FTIR, CSLM, and AFM to ascertain morphology, crystallinity, and composition. For the first time, we studied the kinetic of crystallization with in situ SAXS/WAXS, demonstrating that the co-presence of MNPs and enzymes can induce a faster crystallization when compared with HRP@ZIF-8 and MNP@ZIF-8.…”

Lipase Immobilized Metal‐Organic Frameworks as Remarkably Biocatalyst for Ester Hydrolysis: A One Step Approach for Lipase Immobilization

“…The high porosity and tunable properties of MOFs make them a promising material for a number of applications, including gas storage, drug delivery, catalysis, sensing and adsorption . In the past few years, a number of groups including ours have explored the use of different MOFs like ZIF‐8, Tb‐TATB meso‐MOF, MIL‐ 88B‐NH 2 and UiO‐66 for enzyme immobilization, showing many excellent results towards enzyme based catalytic reactions . Owing to their large surface area and porosity, we believe that MOFs show high potential for encapsulating enzymes and proves themselves as a better support for enzyme immobilization.…”