ArticleScientific reports2021
Self-assembling thermostable chimeras as new platform for arsenic biosensing.
Article in Scientific reports, 2021. 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, 17 citations in OpenAlex.
- Fungal Frontiers in (Bio)sensing.Biosensors · 2026Review
- Biotechnological Potential of Extremophiles: Environmental Solutions, Challenges, and Advancements.Biology · 2025Review
- Extremozyme-Based Biosensors for Environmental Pollution Monitoring: Recent Developments.Biosensors · 2024Review
- A New Strategy for As(V) Biosensing Based on the Inhibition of the Phosphatase Activity of the Arsenate Reductase fromInternational journal of molecular sciences · 2022Article
- Innovative surface bio-functionalization by fungal hydrophobins and their engineered variants.Frontiers in molecular biosciences · 2022Review
- Bio-fabrication of thermozyme-based nano-biosensors: their components and present scenario.Journal of materials science. Materials in electronics · 2022Article
- Article
- Extremophiles, a Nifty Tool to Face Environmental Pollution: From Exploitation of Metabolism to Genome Engineering.International journal of environmental research and public health · 2021Review
- Immobilization of Antibodies by Genetic Fusion to a Fungal Self-Assembling Adhesive Protein.Frontiers in molecular biosciences · 2021Article
- Genomic Insight ofFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The correct immobilization and orientation of enzymes on nanosurfaces is a crucial step either for the realization of biosensors, as well as to guarantee the efficacy of the developed biomaterials. In this work we produced two versions of a chimeric protein, namely ArsC-Vmh2 and Vmh2-ArsC, which combined the self-assembling properties of Vmh2, a hydrophobin from Pleurotus ostreatus, with that of TtArsC, a thermophilic arsenate reductase from Thermus thermophilus; both chimeras were heterologously expressed in Escherichia coli and purified from inclusion bodies. They were characterized for their enzymatic capability to reduce As(V) into As(III), as well as for their immobilization properties on polystyrene and gold in comparison to the native TtArsC. The chimeric proteins immobilized on polystyrene can be reused up to three times and stored for 15 days with 50% of activity loss. Immobilization on gold electrodes showed that both chimeras follow a classic Langmuir isotherm model towards As(III) recognition, with an association constant (K
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.