The enzyme immobilization technology has become a key tool in the field of enzyme applications; however, improving the activity recovery and stability of the immobilized enzymes is still challenging. Herein, we employed a magnetic carboxymethyl cellulose (MCMC) nanocomposite modified with ionic liquids (ILs) for covalent immobilization of lipase, and used Ca-based metal-organic frameworks (MOFs) as the support skeleton and protective layer for immobilized enzymes. The ILs contained long side chains (eight CH units), which not only enhanced the hydrophobicity of the carrier and its hydrophobic interaction with the enzymes, but also provided a certain buffering effect when the enzyme molecules were subjected to compression. Compared to free lipase, the obtained CaBPDC@PPL-IL-MCMC exhibited higher specific activity and enhanced stability. In addition, the biocatalyst could be easily separated using a magnetic field, which is beneficial for its reusability. After 10 cycles, the residual activity of CaBPDC@PPL-IL-MCMC could reach up to 86.9%. These features highlight the good application prospects of the present immobilization method.
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http://dx.doi.org/10.1016/j.colsurfb.2024.113836 | DOI Listing |
Crit Rev Anal Chem
January 2025
Department of Chemistry, University of Delhi, New Delhi, India.
Heavy metal pollution is a major environmental and health problem due to the toxicity and persistence of metals such as lead, mercury, cadmium, and arsenic in water, soil, and air. Advances in sensor technology have significantly improved the detection and quantification of heavy metals, providing real-time monitoring and mitigation tools. This review explores recent developments in heavy metal detection, focusing on innovative uses of immobilized chromogenic reagents, nanomaterials, perovskites, and nanozymes.
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 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.
View Article and Find Full Text PDFSci Rep
January 2025
Department of Nanotechnology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran.
Herein, an efficient and feasible approach was developed to oxidize low-cost agricultural waste (quinoa husk, QS) for the synthesis of carboxylated nanocellulose (CNC). The as-prepared rod-like CNCs (average diameter of 10 nm and length of 103 nm) with a high specific surface area (173 m/g) were utilized for the immobilization of a model protease enzyme (PersiProtease1) either physically or via covalent attachment. For chemical immobilization, CNCs were firstly functionalized with N, N'-dicyclohexylcarbodiimide (DCC) to provide DCNCs nanocarrier which could covalently bond to enzyme trough nucleophilic substitution reaction and formation of the amide bond between DCNCs and enzyme.
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