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This study developed a novel cholesterol biosensing system based on interfacial self-assembled ChOx/HRP dual-enzyme proteinosomes, eliminating the need for complex synthesis. The immobilization of ChOx and HRP on the proteinosome surface enhanced enzyme stability, while the confined spatial proximity of the enzymes significantly improved cascade reaction efficiency, enabling rapid and highly sensitive cholesterol detection.
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http://dx.doi.org/10.1039/d5cc02979a | DOI Listing |
Chem Commun (Camb)
August 2025
State Key Laboratory of Flexible Electronics (LoFE) & Institute of Advanced Materials (IAM), Nanjing University of Posts & Telecommunications, Nanjing, Jiangsu, China.
This study developed a novel cholesterol biosensing system based on interfacial self-assembled ChOx/HRP dual-enzyme proteinosomes, eliminating the need for complex synthesis. The immobilization of ChOx and HRP on the proteinosome surface enhanced enzyme stability, while the confined spatial proximity of the enzymes significantly improved cascade reaction efficiency, enabling rapid and highly sensitive cholesterol detection.
View Article and Find Full Text PDFAnal Bioanal Chem
December 2007
Biomolecular Electronics and Conducting Polymer Research Group, National Physical Laboratory, Dr K.S. Krishnan Marg, New Delhi, 110012, India.
Cholesterol oxidase (ChOx), cholesterol esterase (ChEt), and horseradish peroxidase (HRP) have been co-immobilized covalently on a self-assembled monolayer (SAM) of N-(2-aminoethyl)-3-aminopropyltrimethoxysilane (AEAPTS) deposited on an indium-tin-oxide (ITO) glass surface. These enzyme-modified (ChOx-ChEt-HRP/AEAPTS/ITO) biosensing electrodes have been used to estimate cholesteryl oleate from 10 to 500 mg dL(-1). The sensitivity, Km value, and shelf-life of these ChEt-ChOx-HRP/AEAPTS/ITO biosensing electrodes have been found to be 124 nA mg(-1) dL, 95.
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