In Situ Enzyme Encapsulation in Conductive Layered Double Hydroxides with Enhanced Activity and Stability for a...

Area of Science:

• Biocatalysis and Enzyme Engineering
• Materials Science and Nanotechnology
• Biosensor Development

Background:

• Enzyme immobilization is key for biocatalysis, but improving both stability and activity simultaneously is challenging.
• Existing methods often compromise enzyme performance, limiting practical applications.
• Layered Double Hydroxides (LDHs) offer a promising matrix for enzyme encapsulation.

Purpose of the Study:

• To develop a mild in situ encapsulation strategy for enzymes using LDHs.
• To enhance enzyme stability, activity, and reusability.
• To create a sensitive electrochemical biosensor for hydrogen peroxide (H₂O₂) detection.

Main Methods:

• In situ encapsulation of Horseradish Peroxidase (HRP) within MgAl-LDH matrix.
• Fabrication of an electrochemical sensor using the HRP@MgAl-LDH composite.
• Electrochemical characterization and performance evaluation for H₂O₂ detection.

Main Results:

• The HRP@MgAl-LDH composite maintained native enzyme conformation and showed enhanced structural stability.
• The LDH matrix provided a biocompatible microenvironment, sustaining high enzymatic activity and reusability.
• The developed sensor demonstrated sensitive H₂O₂ detection with a wide linear range, low detection limit, rapid response, and anti-interference capabilities.

Conclusions:

• LDH-based in situ encapsulation effectively balances enzyme activity and stability, overcoming limitations of traditional methods.
• This strategy provides a promising approach for developing practical point-of-care devices for H₂O₂ detection in complex biological samples.
• The high conductivity of the material facilitates efficient electron transfer for enhanced biosensing performance.