Preparation of pullulanase/Cu3(PO4)2 hybrid nanoflower and its catalytic performance as an immobilized enzyme

BİLGİ M., PEKSEL A.

International Journal of Biological Macromolecules, cilt.287, 2025 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 287
  • Basım Tarihi: 2025
  • Doi Numarası: 10.1016/j.ijbiomac.2024.138506
  • Dergi Adı: International Journal of Biological Macromolecules
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, EMBASE, Food Science & Technology Abstracts, INSPEC, Veterinary Science Database
  • Anahtar Kelimeler: Hybrid nanoflower, Immobilized enzyme, Pullulanase
  • Yıldız Teknik Üniversitesi Adresli: Evet

Özet

A commercially important pullulanase enzyme that hydrolyzes α-1,6 glycosidic linkages in pullulan was immobilized as pullulanase/Cu3(PO4)2 hybrid nanoflower. Free and immobilized enzymes both showed the highest activity at 25 °C. The optimum pH of the free enzyme was 4.5, and the immobilized enzyme was 5.5. Immobilization provided the enzyme with good thermal and pH stability. Even after 18 weeks, immobilized enzyme stored at 4 or −20 °C still have 40 % and 60 % activity, respectively. The reusability of the immobilized enzyme was very good with nearly 75 % activity after 8 cycles. Immobilization provided good protection against Cu2+, which is one of the main inhibitors of the pullulanase.