Qualitative enzymatic detection of organophosphate and carbamate insecticides


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Nartop D., Hasanoğlu Özkan E., Yetim N. K. , Sarı N.

JOURNAL OF ENVIRONMENTAL SCIENCE AND HEALTH PART B-PESTICIDES FOOD CONTAMINANTS AND AGRICULTURAL WASTES, vol.55, pp.951-958, 2020 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 55
  • Publication Date: 2020
  • Doi Number: 10.1080/03601234.2020.1797425
  • Journal Name: JOURNAL OF ENVIRONMENTAL SCIENCE AND HEALTH PART B-PESTICIDES FOOD CONTAMINANTS AND AGRICULTURAL WASTES
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, PASCAL, Agricultural & Environmental Science Database, Analytical Abstracts, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Compendex, EMBASE, Environment Index, Food Science & Technology Abstracts, Geobase, Greenfile, MEDLINE, Pollution Abstracts, Veterinary Science Database
  • Page Numbers: pp.951-958
  • Keywords: Acetylcholinesterase, carbamate, organophosphate, polymers containing azomethine, tris(2-aminoethyl)amine polymer-bound, ACETYLCHOLINESTERASE, IMMOBILIZATION, PESTICIDES, BIOSENSORS, SELECTIVITY, STABILITY
  • Gazi University Affiliated: Yes

Abstract

In this study, new polymers containing amides (TrisPS-Ntaa, and TrisPS-Ntaa-Fc) were synthesized by condensation reaction for qualitative identification of insecticides. The synthesized polymers, including amides were investigated by infrared spectroscopy (IR), scanning electron microscopy-energy dispersion X- ray spectrometry (SEM-EDX), and gel permeation chromatography (GPC). Then, acetylcholinesterase enzyme (AChE) was covalently immobilized on these polymers to improve properties (including activity, reusability, and storage stability). Accordingly, organophosphate (malathion, acephate, chlorpyrifos methyl) and carbamate (carbofuran, methiocarb, methomyl), which are used to prevent harmful organisms in some agricultural products were enzymatically determined based on their inhibitory activity on AChE.