دورية أكاديمية
Novel biohybrids of layered double hydroxide and lactate dehydrogenase enzyme: Synthesis, characterization and catalytic activity studies
| العنوان: | Novel biohybrids of layered double hydroxide and lactate dehydrogenase enzyme: Synthesis, characterization and catalytic activity studies |
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| المؤلفون: | Djebbi, Mohamed Amine, Braiek, Mohamed, Hidouri, Slah, Namour, Philippe, Jaffrezic-Renault, Nicole, Amara, Abdesslem Ben Haj |
| المساهمون: | ISA-Interfaces & biosensors - Interfaces & biocapteurs, Institut des Sciences Analytiques (ISA), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS), Lab Phys Mat Lamellaires & Nanomat Hybrides (PMLNM), Université de Carthage (Tunisie) (UCAR), Milieux aquatiques, écologie et pollutions (UR MALY), Institut national de recherche en sciences et technologies pour l'environnement et l'agriculture (IRSTEA), River Monitoring & Management - Suivi et gestion des rivières (2014-2016) |
| المصدر: | ISSN: 0022-2860. |
| بيانات النشر: | HAL CCSD Elsevier |
| سنة النشر: | 2016 |
| المجموعة: | HAL Lyon 1 (University Claude Bernard Lyon 1) |
| مصطلحات موضوعية: | UREA BIOSENSORS, IMMOBILIZATION, NANOHYBRIDS, DESIGN, FILMS, GLUCOSE-OXIDASE, Enzyme immobilization, Catalytic activity, Bioinorganic system, Layered double hydroxide (LDH), Lactate dehydrogenase (Lac Deh), AMPEROMETRIC BIOSENSOR, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry |
| الوصف: | [Departement_IRSTEA]Eaux ; International audience ; The present work introduces new biohybrid materials involving layered double hydroxides (LDH) and biomolecule such as enzyme to produce bioinorganic system. Lactate dehydrogenase (Lac Deh) has been chosen as a model enzyme, being immobilized onto MgAl and ZnAl LDH materials via direct ion-exchange (adsorption) and co-precipitation methods. The immobilization efficiency was largely dependent upon the immobilization methods. A comparative study shows that the co-precipitation method favors the immobilization of great and tunable amount of enzyme. The structural behavior, chemical bonding composition and morphology of the resulting biohybrids were determined by X-ray diffraction (XRD) study, Fourier transform infrared (FTIR) spectroscopy and transmission electron microscopy (TEM), respectively. The free and immobilized enzyme activity and kinetic parameters were also reported using UV-Visible spectroscopy. However, the modified LDH materials showed a decrease in crystallinity as compared to the unmodified LDH. The change in activity of the immobilized lactate dehydrogenase was considered to be due, to the reduced accessibility of substrate molecules to the active sites of the enzyme and the partial conformational change of the Lac Deh molecules as a result of the immobilization way. Finally, it was proven that there is a correlation between structure/microstructure and enzyme activity dependent on the immobilization process. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | hal-01251196; https://hal.science/hal-01251196Test; IRSTEA: PUB00051885 |
| DOI: | 10.1016/j.molstruc.2015.10.065 |
| الإتاحة: | https://doi.org/10.1016/j.molstruc.2015.10.065Test https://hal.science/hal-01251196Test |
| رقم الانضمام: | edsbas.FB156D2B |
| قاعدة البيانات: | BASE |
| DOI: | 10.1016/j.molstruc.2015.10.065 |
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