Enzyme Electrode Immobilization via Modified Thioredoxin
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Solution Overview
Problem
Existing enzyme immobilization techniques on electrodes often result in inappropriate bonding, leading to inefficient enzyme immobilization and reaction efficiency.
Innovation Solution
An enzyme electrode is developed using a modified protein with an amino acid sequence where at least one lysine residue in a fusion protein between thioredoxin reductase and thioredoxin is substituted with a non-lysine amino acid residue, allowing for more appropriate bonding on the electrode surface.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If amino acid side chains of the enzyme are used for immobilization on the electrode, then the enzyme can be immobilized on the electrode surface, but inappropriate bonds are formed leading to reduced reaction efficiency
Solution Approach 1:
The invention changes the chemical parameters of the enzyme by substituting specific amino acid residues (particularly lysine residues at positions 48 and 49 in thioredoxin) with other amino acids. This modification alters the bonding characteristics of the enzyme, enabling it to form appropriate bonds with the electrode surface while maintaining or enhancing catalytic activity, thus resolving the contradiction between reliable immobilization and reaction efficiency
Solution Approach 2:
The invention applies local quality modification by specifically targeting and modifying only certain amino acid residues (positions 48 and 49) within the enzyme structure, while leaving the rest of the enzyme unchanged. This localized modification allows the enzyme to form appropriate bonds at the immobilization site without affecting the overall structure and function of the enzyme, thereby achieving both reliable immobilization and maintained reaction efficiency
Applied Scientific Principles
This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.
Function Achieved in This Case
The modified enzyme electrode achieves improved enzyme immobilization with more appropriate bonds, enhancing reaction efficiency and reducing adverse effects of inappropriate bonding.
Implementation Method 1
a thioredoxin reductase which receives electrons from the electrode and uses the electrons as reducing power to reduce an oxidized thioredoxin into a reduced thioredoxin
Implementation Method 2
a thioredoxin in a reduced state reduces a disulfide bond of a target protein to induce a structural change
Implementation Method 3
an enzyme is immobilized on a surface of the electrode through chemical bonding
Data Source
AI summary
The present disclosure provides, among other features, an enzyme electrode in which an enzyme is immobilized via more appropriate bonds. An enzyme electrode according to the present disclosure includes an electrode and a modified protein having an amino acid sequence obtained by substituting at least one lysine residue in a fusion protein between a thioredoxin reductase and a thioredoxin with a non-lysine amino acid residue, in which the modified protein is immobilized on a surface of the electrode.