JOURNAL ARTICLE

Covalent Immobilization of α-Glucosidase Enzyme onto Amine Functionalized Multi-walled Carbon Nanotubes

Abstract

α-glucosidase (AG) enzyme was immobilized onto amine functionalized multi-walled carbon nanotubes (MWCNTs-NH<sub>2</sub>) by treatment with cross linkers, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS) via amide bonding. The immobilized AG was characterized by Fourier Transform Infrared Spectroscopy (FTIR) and Scanning Electron Microscope (SEM). The performance of the electrode was evaluated by Spectrophotometric method and cyclic voltammetric (CV) method using p-nitrophenyl-α-D-glucopyranoside (PNPG) as a substrate. The immobilized AG enzyme retains about 84.16% activity of its initial response even after 30 days when stored at 4<sup>°</sup>C.

Keywords:
Fourier transform infrared spectroscopy Carbodiimide Cyclic voltammetry Amine gas treating Carbon nanotube Covalent bond Immobilized enzyme Substrate (aquarium) Scanning electron microscope Surface modification Amide Materials science Nuclear chemistry Electrochemistry Chemistry Electrode Polymer chemistry Chemical engineering Organic chemistry Enzyme Nanotechnology Physical chemistry Composite material

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Citation History

Topics

Electrochemical sensors and biosensors
Physical Sciences →  Engineering →  Electrical and Electronic Engineering
Enzyme Catalysis and Immobilization
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Molecular Biology
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