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Naji, M. |
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Motta, Antonella |
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Aletan, Dirar |
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Mohamed, Tarek |
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Ertürk, Emre |
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Taccardi, Nicola |
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Kononenko, Denys |
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Petrov, R. H. | Madrid |
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Alshaaer, Mazen | Brussels |
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Bih, L. |
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Casati, R. |
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Muller, Hermance |
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Kočí, Jan | Prague |
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Šuljagić, Marija |
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Kalteremidou, Kalliopi-Artemi | Brussels |
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Azam, Siraj |
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Ospanova, Alyiya |
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Blanpain, Bart |
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Ali, M. A. |
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Popa, V. |
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Rančić, M. |
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Ollier, Nadège |
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Azevedo, Nuno Monteiro |
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Landes, Michael |
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Rignanese, Gian-Marco |
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Tsuzuki, Takuya
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Publications (7/7 displayed)
- 2022Paper-Like Writable Nanoparticle Network Sheets for Mask-Less MOF Patterningcitations
- 2020Janus conductive/insulating microporous ion-sieving membranes for stable Li-S batteriescitations
- 2019Reduction kinetics for large spherical 2:1 iron–manganese oxide redox materials for thermochemical energy storagecitations
- 2019Metal-Organic Frameworks/Conducting Polymer Hydrogel Integrated Three-Dimensional Free-Standing Monoliths as Ultrahigh Loading Li-S Battery Electrodescitations
- 2018NiO–ZnO Nanoheterojunction Networks for Room-Temperature Volatile Organic Compounds Sensingcitations
- 2017Removal of lead from aqueous solution using superparamagnetic palygorskite nanocompositecitations
- 2013Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostabilitycitations
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article
Immobilization of β-glucosidase on a magnetic nanoparticle improves thermostability
Abstract
<p>The objective of the present work was to develop a thermostable β-glucosidase through immobilization on a nanoscale carrier for potential application in biofuel production. β-Glucosidase (BGL) from Aspergillus niger was immobilized to functionalized magnetic nanoparticles by covalent binding. Immobilized nanoparticles showed 93% immobilization binding. Immobilized and free BGL were characterized using Transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FTIR) techniques. Free and immobilized enzyme exhibited different pH-optima at pH 4.0 and 6.0, respectively, but had the same temperature optima at 60°C. Michaelis constant (K<sub>M</sub>) was 3.5 and 4.3mM for free and immobilized BGL. Thermal stability of the immobilized enzyme was enhanced at 70°C. The immobilized nanoparticle-enzyme conjugate retained more than 50% enzyme activity up to the 16th cycle. Maximum glucose synthesis from cellobiose hydrolysis by immobilized BGL was achieved at 16h.</p>