Molecular 'wiring' of plasma amine oxidase: Green and enzyme friendly approaches
Autor: | Eugene Kang, Tae-Hoon Kim, Sabrina Belbekhouche, Mihaela D. Leonida |
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Přispěvatelé: | Institut de Chimie et des Matériaux Paris-Est (ICMPE), Institut de Chimie du CNRS (INC)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), McGill University Research Centre on Complex Traits [Montreal] (MRCCT), McGill University = Université McGill [Montréal, Canada] |
Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
Benzylamines
congenital hereditary and neonatal diseases and abnormalities Amine oxidase Ionic Liquids Biosensing Techniques 02 engineering and technology Biochemistry Redox Antioxidants 03 medical and health sciences chemistry.chemical_compound Structural Biology Spectroscopy Fourier Transform Infrared Electrochemistry Pressure [CHIM]Chemical Sciences Monoamine Oxidase Molecular Biology ComputingMilieux_MISCELLANEOUS 030304 developmental biology chemistry.chemical_classification 0303 health sciences biology Green Chemistry Technology General Medicine respiratory system 021001 nanoscience & nanotechnology Combinatorial chemistry Enzyme assay Freeze Drying Enzyme chemistry Reagent Ionic liquid biology.protein bacteria Amine gas treating 0210 nano-technology Biosensor Copper |
Zdroj: | International Journal of Biological Macromolecules International Journal of Biological Macromolecules, Elsevier, 2020, 165, pp.2071-2078. ⟨10.1016/j.ijbiomac.2020.10.082⟩ |
ISSN: | 0141-8130 |
Popis: | The study describes two approaches to enhance oxidoreductases. Both target molecular “wiring” of enzymes using green processes. The concepts were tested on plasma amine oxidase (PAO). In the first procedure PAO was transiently exposed to an ionic liquid (IL) in the presence of redox molecules, which resulted in partial unfolding. During subsequent dialysis, the enzyme refolded entrapping redox units and affording shorter distances for electron tunneling, hence a molecular “wire” to PAO's prosthetic groups. The other procedure described herein was totally reagentless, using high hydraulic pressure (HHP) to partially denature PAO (in the presence of redox molecules) followed by dialysis and refolding. The two approaches to enzyme “wiring” are discussed comparatively from the point of view of the parameters used during the procedure, residual enzyme activity, nature of the modifier, interaction between PAO and the redox molecules, and stability over time. The most active modified PAO (PAO-ME) from each series was tested in a biosensor for amine detection, toward applications in the food industry and clinical laboratory. Our approaches used “green” reagents (IL) and were made enzyme-friendly as well by the choice of “wires”. |
Databáze: | OpenAIRE |
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