Inhibitory Effects of Chitosan-Silver Nanoparticles on Acetylcholinesterase from the Black Bean Aphid

Authors

  • Abubakar Musa Department of Biochemistry, College of Natural and Applied Sciences, Al-Qalam University Katsina, P.M.B. 2137, Katsina, Nigeria.
  • Aminu Usman Department of Biochemistry, Faculty of Natural and Applied Sciences, Umaru Musa Yar’adua University, P.M.B. 2218, Katsina, Katsina State, Nigeria.
  • Ibrahim Hamza Kankia Department of Biochemistry, Faculty of Natural and Applied Sciences, Umaru Musa Yar’adua University, P.M.B. 2218, Katsina, Katsina State, Nigeria.
  • S.A. Akilu Department of Biochemistry, Faculty of Natural and Applied Sciences, Umaru Musa Yar’adua University, P.M.B. 2218, Katsina, Katsina State, Nigeria.
  • Evans Egwim Department of Biochemistry, School of Life Sciences, Federal University of Technology Minna, P.M.B. 65, Minna, Niger State, Nigeria.

DOI:

https://doi.org/10.54987/jemat.v14i1.212

Keywords:

Chitosan, Fish scale waste, Silver nanoparticles, Acetylcholinesterase, Green synthesis

Abstract

This study examined chitosan recovered from fish-scale waste, the synthesis of chitosan-silver nanoparticles (Ch-AgNPs), and their inhibition of acetylcholinesterase (AChE) from the black bean aphid, Aphis fabae. Fish scales were demineralized, deproteinized, and deacetylated under different solid-to-alkali ratios and temperatures. The resulting material and Ch-AgNP preparations were characterized by yield, pH, viscosity, water-binding capacity, fat-binding capacity, degree of deacetylation, and Fourier-transform infrared spectroscopy. The highest recorded chitosan yield (46.686%) occurred at a fish-scale-to-NaOH ratio of 1:2 and 55 °C. The degree of deacetylation ranged from 21.533% to 57.593%. Aphid AChE was purified by ammonium sulfate precipitation, DEAE-52 ion-exchange chromatography, and Superdex 200 gel filtration. The final preparation had a specific activity of 24.53 U mg−1, a reported purification fold of 229.40, and a recovery of 13.99%. Crude and purified AChE showed temperature optima near 30 °C; their pH optima were 7.0 and 7.5, respectively. Ch-AgNP preparations inhibited both enzyme preparations, although the IC50 pattern was not monotonic across the five formulations. These findings support further evaluation of fish-scale-derived Ch-AgNPs as enzyme-targeted materials, with additional nanoparticle characterization and bioassays needed before pesticidal efficacy can be established.

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Published

31.07.2026

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How to Cite

Inhibitory Effects of Chitosan-Silver Nanoparticles on Acetylcholinesterase from the Black Bean Aphid. (2026). Journal of Environmental Microbiology and Toxicology, 14(1), 12-17. https://doi.org/10.54987/jemat.v14i1.212