Purification of acetylcholinesterase from Halyomorpha halys (Stål) (Heteroptera: Pentatomidae) and management of control of the Pest through inhibition of the enzyme


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DİNÇER B., Akpınar H.

International Journal of Tropical Insect Science, cilt.43, sa.5, ss.1421-1429, 2023 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 43 Sayı: 5
  • Basım Tarihi: 2023
  • Doi Numarası: 10.1007/s42690-023-01047-x
  • Dergi Adı: International Journal of Tropical Insect Science
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Agricultural & Environmental Science Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Food Science & Technology Abstracts, Veterinary Science Database
  • Sayfa Sayıları: ss.1421-1429
  • Anahtar Kelimeler: Acetylcholinesterase, Halyomorpha halys, Inhibition, Pest, Purification
  • Recep Tayyip Erdoğan Üniversitesi Adresli: Evet

Özet

Halyomorpha halys (Stål) (Heteroptera: Pentatomidae) has brought about agricultural harm throughout the Eastern Black Sea coastline since 2017. It continues to come to a threat because there are no adequate studies on managing this pest. One of the major rein strategies of insecticides is acetylcholinesterase (ACHE) inhibition. Therefore, this study aims to investigate an alternative way to struggle H. halys by inhibiting ACHE. The ACHE was purified from H. halys using edrophonium-Sepharose 6B affinity chromatography and characterized by examining some kinetic properties. The molecular weight of the purified enzyme was determined by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis and natural polyacrylamide gel electrophoresis. In addition, the inhibitory effects of tacrine and edrophonium chloride, and water extracts of olive leaf, walnut leaf and alder leaf on this ACHE were investigated. The acetylcholinesterase was purified 403-fold with an 83.3% yield. H. halys ACHE was found to have six subunits and a molecular weight of approximately 350 kDa. The ACHE’s K m, V max, and k cat values were assigned to be 0.02 ± 0.006 mM, 3,333.3 ± 481 EU.mg protein− 1, and 1070.2 ± 184 min− 1, respectively. All inhibitors highly inhibited of activity of h.halys ACHE. Especially, the fact that the water extracts of these plants are effective in ACHE inhibition is significant due to being environmentally amicable pesticides that may be benefited in the struggle with the pest.