ArticleAnalytica chimica acta2015
Chemically glycosylation improves the stability of an amperometric horseradish peroxidase biosensor.
Article in Analytica chimica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 39 citations in OpenAlex.
- Comparison of two peroxidases with high potential for biotechnology applications - HRPComputational and structural biotechnology journal · 2024Article
- Road Map of Semiconductor Metal-Oxide-Based Sensors: A Review.Sensors (Basel, Switzerland) · 2023Review
- The Effect of a Rotating Cone on Horseradish Peroxidase Aggregation on Mica Revealed by Atomic Force Microscopy.Micromachines · 2022Article
- Graphene nanosheet-sandwiched platinum nanoparticles deposited on a graphite pencil electrode as an ultrasensitive sensor for dopamine.RSC advances · 2022Article
- Effect ofComputational and structural biotechnology journal · 2022Article
- An Overview on Recent Progress of Metal Oxide/Graphene/CNTs-Based Nanobiosensors.Nanoscale research letters · 2021Review
- Metal Oxides-Based Semiconductors for Biosensors Applications.Frontiers in chemistry · 2020Review
- Colorimetric Glucose Assay Based on Magnetic Particles Having Pseudo-peroxidase Activity and Immobilized Glucose Oxidase.Molecular biotechnology · 2016Article
- Graphene oxide as a protein matrix: influence on protein biophysical properties.Journal of nanobiotechnology · 2015Article
- Biocompatible ZnS:Mn quantum dots for reactive oxygen generation and detection in aqueous media.Journal of nanoparticle research : an interdisciplinary forum for nanoscale science and technologyArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We constructed a biosensor by electrodeposition of gold nano-particles (AuNPs) on glassy carbon (GC) and subsequent formation of a 4-mercaptobenzoic acid self-assembled monolayer (SAM). The enzyme horseradish peroxidase (HRP) was then covalently immobilized onto the SAM. Two forms of HRP were employed: non-modified and chemically glycosylated with lactose. Circular dichroism (CD) spectra showed that chemical glycosylation did neither change the tertiary structure of HRP nor the heme environment. The highest sensitivity of the biosensor to hydroquinone was obtained for the biosensor with HRP-lactose (414 nA μM(-1)) compared to 378 nA μM(-1) for the one employing non-modified HRP. The chemically glycosylated form of the enzyme catalyzed the reduction of hydroquinone more rapidly than the native form of the enzyme. The sensor employing lactose-modified HRP also had a lower limit of detection (74 μM) than the HRP biosensor (83 μM). However, most importantly, chemically glycosylation improved the long-term stability of the biosensor, which retained 60% of its activity over a four-month storage period compared to only 10% for HRP. These results highlight improvements by an innovative stabilization method when compared to previously reported enzyme-based biosensors.
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