Evidence map›Paper›PMID 33191461›Full record

ArticleApplied microbiology and biotechnology2021

A novel biosensor for the detection of organophosphorus (OP)-based pesticides using organophosphorus acid anhydrolase (OPAA)-FL variant.

Monika Jain, Priyanka Yadav, Bhavana Joshi, Abhijeet Joshi, Prashant Kodgire

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Construction of a ratiometric fluorescent sensing platform based on near-infrared carbon dots for organophosphorus pesticides detection.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2023
    Article
  3. Article
  4. Article
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Monika JainDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Khandwa Road, Indore, India.
Priyanka YadavDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Khandwa Road, Indore, India.
Bhavana JoshiDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Khandwa Road, Indore, India.
Abhijeet JoshiDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Khandwa Road, Indore, India. abhijeet.joshi@iiti.ac.in.
Prashant KodgireDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Khandwa Road, Indore, India. pkodgire@iiti.ac.in.ORCID http://orcid.org/0000-0003-3334-2114
Indian Institute of Technology Indore · IN

Funding

Department of Biotechnology, Govt. of India BT/PR20319/BBE/117/189/2016Department of Biotechnology, Govt. of India BT/PR24652/NER/95/795/2017DST-INSPIRE IF170325
6 · The paper itself

Abstract

Indiscriminate use of organophosphorus (OP)-based insecticides is a great concern to human health because of bioaccumulation-induced health hazards. Potentially fatal consequences and limited treatment methods of OP poisoning necessitate the need for the development of reliable, selective, cost-effective, and sensitive methods of OP detection. To tackle this issue, the development of effective devices and methods is required to sensitively detect as well as degrade OPs. Enzymatic sensor systems have gained popularity due to high catalytic activity, enhanced detection limits, and high sensitivity with the environmentally benign operation. Organophosphorus acid anhydrolase (OPAA) from Alteromonas sp. JD6.5 is capable of hydrolyzing the P-F, P-O, P-S, and P-CN bonds, in OPs, including nerve agents of the G/V-series. Several mutants of OPAA are reported which have greater activity against various OPs. In this study, recombinant expression of the OPAA-FL variant in Escherichia coli was performed, purified, and subsequently tested for activity against ethyl paraoxon. OPAA-FL variant showed its optimum activity at pH 8.5 and 50 °C. Colorimetric and fluorometric assays were used for estimation of ethyl paraoxon based on p-nitrophenol and fluorescein isothiocyanate (FITC) fluorescence intensity, respectively. Colorimetric and fluorometric assay estimation indicates that ethyl paraoxon can be estimated in the linear range of 0.01 to 1 mM and 0.1 to 0.5 mM, with LOD values 0.04 mM and 0.056 mM, respectively. Furthermore, the OPAA-FL variant was immobilized into alginate microspheres for colorimetric detection of ethyl paraoxon and displayed a linear range of 0.025 to 1 mM with a LOD value of 0.06 mM. KEY POINTS: • Biosensing of paraoxon with purified and encapsulated OPAA-FL variant. • Colorimetric and fluorometric biosensing assay developed using OPAA-FL variant for paraoxon. • First report on alginate encapsulation of OPAA-FL variant for biosensing of paraoxon. Graphical abstract.

Indexed as

AlteromonasBiosensing TechniquesPesticidesAryldialkylphosphataseColorimetryOrganophosphorus CompoundsParaoxonAryldialkylphosphataseOrganophosphorus CompoundsParaoxonPesticidesAcetylcholinesterase (AChE)Organophosphorus acid anhydrolase (OPAA)-FL variantOrganophosphorus compounds (OPs)Paraoxon

Identifiers

PMID33191461
OpenAlexW3099864789

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.