A novel nanoplatform encapsulating glucose oxidase for spectrophotometric biosensing of hydrogen peroxide and glucose. Issue 3 (19th December 2019)
- Record Type:
- Journal Article
- Title:
- A novel nanoplatform encapsulating glucose oxidase for spectrophotometric biosensing of hydrogen peroxide and glucose. Issue 3 (19th December 2019)
- Main Title:
- A novel nanoplatform encapsulating glucose oxidase for spectrophotometric biosensing of hydrogen peroxide and glucose
- Authors:
- Pezhhan, Hamzeh
Akhond, Morteza
Shamsipur, Mojtaba - Abstract:
- Abstract : Inspired by the role of the chelation of Fe 3+ –catechol in inter-protein interactions and the production of adhesives by marine mussels, we used DA as an anchor to connect GOx to Fe3 O4 magnetic nanoparticle cores via the formation of Fe(OH)3 shells. Abstract : In this work, we were inspired from the role of chelation of Fe 3+ –catechol in inter-protein interactions and the production of adhesives by marine mussels, and used dopamine (DA) as an anchor to connect the enzyme glucose oxidase (GOx) to Fe3 O4 magnetic nanoparticle cores via the formation of Fe(OH)3 shells. Because of the tendency of catechol and similar ligands such as DA to coordinate with the Fe 3+ surface sites, a tight binding of DA to the Fe3 O4 –Fe(OH)3 core–shell was easily accomplished. Accordingly, we formulated an Fe 3+ –polyDA framework to encapsulate GOx; we specifically produced Fe3 O4 –Fe(OH)3 @GOx–polyDA by carrying out an in situ polymerization of DA covalently linked to GOx on the Fe(OH)3 shells of magnetic nanoparticles. The Fe 3+ –polyDA framework stabilized the structure of the encapsulated GOx layer and increased its thermal stability, operational stability and recyclability, while preserving its activity. The prepared Fe3 O4 –Fe(OH)3 @GOx–polyDA probe displaying enzyme-like characteristics was used as a multifunctional platform in a sensitive and selective spectrophotometric biosensor, with N, N -diethyl- p -phenylenediamine sulfate (DPD) as a redox indicator, for sub-micromolarAbstract : Inspired by the role of the chelation of Fe 3+ –catechol in inter-protein interactions and the production of adhesives by marine mussels, we used DA as an anchor to connect GOx to Fe3 O4 magnetic nanoparticle cores via the formation of Fe(OH)3 shells. Abstract : In this work, we were inspired from the role of chelation of Fe 3+ –catechol in inter-protein interactions and the production of adhesives by marine mussels, and used dopamine (DA) as an anchor to connect the enzyme glucose oxidase (GOx) to Fe3 O4 magnetic nanoparticle cores via the formation of Fe(OH)3 shells. Because of the tendency of catechol and similar ligands such as DA to coordinate with the Fe 3+ surface sites, a tight binding of DA to the Fe3 O4 –Fe(OH)3 core–shell was easily accomplished. Accordingly, we formulated an Fe 3+ –polyDA framework to encapsulate GOx; we specifically produced Fe3 O4 –Fe(OH)3 @GOx–polyDA by carrying out an in situ polymerization of DA covalently linked to GOx on the Fe(OH)3 shells of magnetic nanoparticles. The Fe 3+ –polyDA framework stabilized the structure of the encapsulated GOx layer and increased its thermal stability, operational stability and recyclability, while preserving its activity. The prepared Fe3 O4 –Fe(OH)3 @GOx–polyDA probe displaying enzyme-like characteristics was used as a multifunctional platform in a sensitive and selective spectrophotometric biosensor, with N, N -diethyl- p -phenylenediamine sulfate (DPD) as a redox indicator, for sub-micromolar detection of hydrogen peroxide and glucose via an enzymatic cascade reaction. … (more)
- Is Part Of:
- Analytical methods. Volume 12:Issue 3(2020)
- Journal:
- Analytical methods
- Issue:
- Volume 12:Issue 3(2020)
- Issue Display:
- Volume 12, Issue 3 (2020)
- Year:
- 2020
- Volume:
- 12
- Issue:
- 3
- Issue Sort Value:
- 2020-0012-0003-0000
- Page Start:
- 345
- Page End:
- 357
- Publication Date:
- 2019-12-19
- Subjects:
- Chemistry, Analytic -- Periodicals
Analytical biochemistry -- Periodicals
Chemical laboratories -- Standards -- Periodicals
543.1905 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/AY ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c9ay02356a ↗
- Languages:
- English
- ISSNs:
- 1759-9660
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0897.103700
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 12685.xml