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An investigation is performed into the efficiency of the HUT 6037 enzyme immobilized in three different mesoporous silicas, namely mesoporous silica film, mesocellular foam, and rod-like SBA-15. It is shown that for all three supports, the pH value changes the surface charge and charge density and hence determines the maximum loading capacity of the enzyme. The products of the enzyme hydrolytic reaction are analyzed by H-NMR. The results show that among the three silica supports, the mesoporous silica film (with a channel length in the range of 60-100 nm) maximizes the accessibility of the immobilized enzyme. The loading capacity of the enzyme is up to 95% at pH 7 and the activity of the immobilized enzyme is maintained for more than 15 days when using a silica film support. The order of the activity of the enzyme immobilized in different mesoporous silica supports is: mesoporous silica film > mesocellular foam > rod-like SBA-15. Furthermore, the immobilized enzyme can be easily separated from the reaction solution simple filtration or centrifugation methods and re-used for hydrolytic reaction as required.
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http://dx.doi.org/10.1039/d1ra01358k | 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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