Preparation and analysis application of electrochemical sensing device based on zinc oxide nano-rod and myoglobin

Abstract

The invention discloses a preparation and an application of an electrochemical sensing device based on zinc oxide nano-rod and myoglobin. The preparation of the electrochemical sensing device comprises the steps of: preparing a base electrode (CILE) using a proper amount of graphite powder and ionic liquid; adding a suitable amount of zinc oxide nanowire solid (ZnONW) with an aspect ratio greaterthan 300 to an agate mortar and uniformly grinding until the zinc oxide nanowire solid becomes white powder with no obvious particulate to obtain zinc oxide nano-rod (ZnONR); dispersing a proper amount of the ZnONR in secondary distilled water so as to prepare dispersion liquid with different concentrations; dissolving a proper amount of myoglobin (Mb) in secondary distilled water to prepare an aqueous solution with a certain concentration; mixing the ZnONR dispersion liquid and the Mb aqueous solution and fully oscillating; drop coating a certain volume of the mixed liquid on the surface of the CILE to obtain Mb-ZnONR/CILE; coating Nafion ethanol solution on the surface of the Mb-ZnONR/CILE surface to obtain the electrochemical sensing device based on zinc oxide nanorods and myoglobin (Nafion/Mb-ZnONR/CILE). According to the preparation and the application of the electrochemical sensing device based on zinc oxide nano-rod and myoglobin, good electrocatalytic performance is shown whenthe sensing device is applied to electrochemical detection of sodium nitrite.

Description

technical field [0001] The invention relates to the preparation and research application of an electrochemical enzyme sensor, in particular to the preparation and analysis application of an electrochemical sensor device based on zinc oxide nanorods and myoglobin. Background technique [0002] Myoglobin (Mb) is a common redox protein, composed of a single polypeptide chain bond (globin) and prosthetic heme, with a relative molecular mass of 17800 and 150-160 amino acid residues. Mb exists more in mammalian cells (mainly muscle cells), and undertakes the work of storing and transporting oxygen. Due to its clear biological structure, it is often used to study the electrochemical behavior of redox proteins and build electrochemical biosensors. However, the peptide chain of Mb is wound into a spherical structure, and the polar amino acid residues are almost all present on the surface of the molecule, making it water-soluble; the non-polar amino acid residues are distributed insi...

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Problems solved by technology

However, the peptide chain of Mb is wound into a spherical structure, and the polar amino acid residues are almost all present on the surface of the molecule, making it water-soluble; the non-polar amino acid residues are distributed inside the molecule, making the inside appear hydrophobic. Its electroactive center heme is deeply buried in the hole, so its direct electron transfer is generally difficult to achieve, and it needs to use a mediator as a bridge to provide an electron transfer channel.

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