High Stability of Immobilized Acetylcholinesterase on Chitosan Beads


IŞIK M.

ChemistrySelect, cilt.5, sa.15, ss.4623-4627, 2020 (SCI-Expanded) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 5 Sayı: 15
  • Basım Tarihi: 2020
  • Doi Numarası: 10.1002/slct.202000559
  • Dergi Adı: ChemistrySelect
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier
  • Sayfa Sayıları: ss.4623-4627
  • Anahtar Kelimeler: Acetylcholinesterase, Chitosan-glutaraldehyde, Immobilization, Inhibitors, Storage stability
  • Bilecik Şeyh Edebali Üniversitesi Adresli: Evet

Özet

The enzymes are unstable and have a short lifetime; this causes a decrease in the number of enzyme usage and increases the cost. In the study, the acetylcholinesterase (AChE) enzyme was covalently immobilized to the surface of chitosan via glutaraldehyde by cross-linking method, where glutaraldehyde contains functional amine group. The immobilized enzyme was characterized by scanning electron microscopy-energy dispersive X-ray analysis (SEM-EDX). The operational and storage stability of immobilized AChE was found higher than the free enzyme by the spectrophotometric method. The storage stability of the immobilized AChE was found 81% for 60 days, while the free AChE lost a high ratio of its activity in 30 days. It was observed that 93% activity was preserved for the immobilized enzyme after reusing it approximately 30 times. Moreover, kinetic parameters, the Km and Vmax, were found 0.073 mM and 0.244 EU/mL for immobilized AChE and 0.044 mM and 0.362 EU/mL for free AChE, respectively. The AChE enzyme is used in the analysis of pesticides; that is why the high stability and reusability of the enzyme as a result of immobilization proses are important in biotechnological applications.