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An enhanced chemiluminescence bioplatform by confining glucose oxidase in hollow calcium carbonate particles.


ABSTRACT: A chemiluminescence (CL) amplification platform based on HCC/Lucigenin&GOx (HLG) film was developed. Hollow structural calcium carbonate (HCC) particles were used as alternative materials for carrying both enzyme and CL reagent. The model enzyme (GOx), immobilized in confined space of HCC particles, exhibited an improved biocatalysis. The Michaelis constant (Km) and the enzymatic rate constant (kcat) were determined to be 0.209??M and 2.21?s(-1), respectively, which are much better than those of either free GOx in aqueous solution or the GOx immobilized on common nanomaterials. Based on the HLG platform, CL signal was effectively amplified and visualized after adding trace glucose, which could be attributed to the HCC particles' high biocompatibility, large specific surface area, attractive interfacial properties and efficient interaction with analyses. The visual CL bioplatform showed an excellent performance with high selectivity, wide linear range and low detection limit for sensing trace glucose. Because it eliminates the need of complicated assembly procedure and enables visualization by the naked eye, the sensitive and selective CL bioplatform would provide wide potential applications in disease diagnosis and food safety.

SUBMITTER: Wang C 

PROVIDER: S-EPMC4832249 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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An enhanced chemiluminescence bioplatform by confining glucose oxidase in hollow calcium carbonate particles.

Wang Congmin C   Zhou Cuisong C   Long Yuyin Y   Cai Honglian H   Yin Cuiyun C   Yang Qiufang Q   Xiao Dan D  

Scientific reports 20160415


A chemiluminescence (CL) amplification platform based on HCC/Lucigenin&GOx (HLG) film was developed. Hollow structural calcium carbonate (HCC) particles were used as alternative materials for carrying both enzyme and CL reagent. The model enzyme (GOx), immobilized in confined space of HCC particles, exhibited an improved biocatalysis. The Michaelis constant (Km) and the enzymatic rate constant (kcat) were determined to be 0.209 μM and 2.21 s(-1), respectively, which are much better than those of  ...[more]

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