MOFs are porous materials with adjustable porosity ensuing a tenable surface area and stability. MOFs consist of metal containing joint where organic ligands are linked with coordination bonding rendering a unique architecture favouring the diverse applications in attachment of enzymes, Chemical catalysis, Gases storage and separation, biomedicals. In the past few years immobilization of soluble enzymes on/in MOF has been the topic of interest for scientists working in diverse field. The activity of enzyme, reusability, storage, chemical and thermal stability, affinity with substrate can be greatly improved by immobilizing of enzyme on MOFs. Along with improvement in enzymes properties, the high loading of enzyme is also observed while using MOFs as immobilization support. In this review a detail study of immobilization on/in Metalorganic Frameworks (MOFs) have been described. Furthermore, strategies for the enzyme immobilization on MOFs and resulting in improved catalytic performance of immobilized enzymes have been reported.
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http://dx.doi.org/10.2174/0929866526666190430120046 | DOI Listing |
Int J Biol Macromol
January 2025
Key Laboratory of Chem-Biosensing of Anhui Province, Key Laboratory of Functional Molecular Solids of Anhui Province, College of Chemistry and Materials Science, Anhui Normal University, Wuhu 241000, Anhui, China. Electronic address:
Adsorption and biodegradation are two important means to remove the pollutants from the environment, but how to combine them and improve the catalytic performance and stability of free enzyme are facing great challenges. Herein, lipase from Candida rugosa (CRL) was immobilized into bimetallic ZnCo-MOF by biomineralization, which not only significantly improved the catalytic activity and stability of CRL but also endowed it with excellent reusability. Furthermore, CRL@ZnCo-MOF established a synergetic system of combined adsorption and enzymatic degradation for the sustainable removal of dibutyl phthalate (DBP) in actual water environment.
View Article and Find Full Text PDFMicrob Cell Fact
January 2025
Botany and Microbiology Department, Faculty of Science, Benha University, Benha, Egypt.
Background: Because the process is cost-effective, microbial pectinase is used in juice clearing. The isolation, immobilization, and characterization of pectinase from Aspergillus nidulans (Eidam) G. Winter (AUMC No.
View Article and Find Full Text PDFSci Rep
January 2025
Faculty of Biotechnology, German International University, Regional Ring Road, East Cairo, New Administrative Capital, Cairo, Egypt.
In the current study, calcium alginate was used as a carrier for Agaricus bisporus CU13 laccase immobilization, with an immobilization yield of the entrapped laccase of 91.95%. Free and immobilized enzymes showed their best enzyme activity at 60 °C as an optimum temperature.
View Article and Find Full Text PDFBiosens Bioelectron
December 2024
Department of Pharmaceutical Analysis, School of Pharmacy, Key Laboratory of Protection, Development and Utilization of Medicinal Resources in Liupanshan Area, Ministry of Education, Ningxia Medical University, Yinchuan, 750004, China. Electronic address:
Efficient analysis of active ingredient in complex natural products is crucial for drug discovery, but developing a simple method for this is challenging. The discovery of drugs against bacterial resistance is urgent because drug-resistant bacteria produce β-lactamases, which inactivate antibiotics and increase infection risks, particularly the AmpC β-lactamase. Here, an integrated analytical model based on colorimetric sensing and magnetic nanoparticles (MNPs) affinity chromatography was developed for screening AmpC β-lactamase inhibitors.
View Article and Find Full Text PDFEnzyme Microb Technol
December 2024
Guangxi Key Laboratory of Natural Polymer Chemistry and Physics, College of Chemistry and Materials, Nanning Normal University, Nanning 530001, PR China.
The immobilization of α-amylase and glucoamylase using a metal-organic framework (enzyme@ZIF-8) was prepared in situ through a one-pot method. The morphology, crystal structure, and molecular characteristics of the free enzyme and enzyme@ZIF-8 were characterized. The enzyme@ZIF-8 exhibited the rhombic dodecahedron morphology, with a decrease in particle size.
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