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The development of efficient enzyme immobilization to promote their recyclability and activity is highly desirable. Zeolitic imidazolate framework-8 (ZIF-8) has been proved to be an effective platform for enzyme immobilization due to its easy preparation and biocompatibility. However, the intrinsic hydrophobic characteristic hinders its further development in this filed. Herein, a facile synthesis approach was developed to immobilize pepsin (PEP) on the ZIF-8 carrier by using Ni ions as anchor (ZIF-8@PEP-Ni). By contrast, the direct coating of PEP on the surface of ZIF-8 (ZIF-8@PEP) generated significant conformational changes. Electrochemical oxygen evolution reaction (OER) was employed to study the catalytic activity of immobilized PEP. The ZIF-8@PEP-Ni composite attains remarkable OER performance with an ultralow overpotential of only 127 mV at 10 mA cm , which is much lower than the 690 and 919 mV overpotential values of ZIF-8@PEP and PEP, respectively.
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http://dx.doi.org/10.1002/anie.202216699 | DOI Listing |
J Agric Food Chem
September 2025
The State Key Laboratory of Food Science and Resources, Jiangnan University, 1800 Lihu Road, Wuxi 214122, China.
This study develops a multienzyme coimmobilization strategy on NTA-functionalized ZIF-8-coated magnetic nanoparticles (NZMNPs) for efficient d-allulose synthesis. Under optimized immobilization conditions (enzyme-to-carrier ratio: 1:50 w/w, 30 min immobilization), the system achieved an immobilization efficiency of 93.7% along with 107.
View Article and Find Full Text PDFSmall
September 2025
State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, 100029, China.
Modifying cells to achieve desired functions has attracted extensive attention in bioengineering and bio-manufacturing. Approaches based on cell-surface engineering have the potential to endow cells with multiple functions and also create a protective shell around them. However, such shells are generally irreversible and lack functionality, leading to various drawbacks associated with irreversible dynamics.
View Article and Find Full Text PDFRSC Adv
September 2025
Department of Chemical Engineering and Green Technology, Institute of Chemical Technology (ICT) Mumbai Maharashtra 400019 India
The sustainable synthesis of bio-based monomers from renewable biomass intermediates is a central goal in green chemistry and biorefinery innovation. This study introduces a synergistic catalytic-enzymatic strategy for the efficient and eco-friendly oxidation of 5-hydroxymethylfurfural (5-HMF) into 2,5-furandicarboxylic acid (FDCA), a key monomer for next-generation biodegradable plastics. The catalytic phase employed non-noble metal catalysts, MnO and Co-Mn supported on activated carbon (Co-Mn/AC), under mild batch reaction conditions at 90 °C.
View Article and Find Full Text PDFMikrochim Acta
September 2025
Faculty of Science, Shenyang University of Chemical Technology, Shenyang, 110142, China.
A sensitive electrochemical glucose biosensor using ZrO₂@CNTs nanocomposite was developed for real-time metabolism monitoring for athletes. The nanocomposite was prepared by a simple ultrasound-assisted technique, and the glucose oxidase (GOx) was covalently immobilized to improve the biorecognition ability. CNTs treated with acid served as a highly conductive framework, and ZrO₂ nanoparticles can provide structural stability and catalytic performance, thus showing synergistic enhancement of electron transfer kinetics and enzyme loading capacity.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
Department of Pharmaceutical Engineering, School of Engineering, China Pharmaceutical University, Nanjing, 211198, China; Engineering Research Center for Smart Pharmaceutical Manufacturing Technologies, Ministry of Education, China Pharmaceutical University, Nanjing, 211198, China. Electronic addres
1,3-Dioleoyl-2-palmitoylglycerol (OPO) is crucial for infant nutrition; however, conventional immobilized lipase requires high-purity enzymes, which increases costs and limits industrial scalability. Herein, Rhizomucor miehei lipase (RML) was immobilized on surface-modified magnetic nanoparticles using cross-linked enzyme aggregates (CLEAs) technology to produce FeO@SiO@TPOAC@RML CLEAs. This approach combines the separation and immobilization of enzymes, allowing for the use of lower-purity lipase, which enhances its suitability for industrial-scale processes.
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