Immobilization of the Bacillus licheniformis α-Amylase on Azole Functionalized Nanoparticle: More Active, Stable, and Usability

Kaptan Usul S., Binay B., Soydan A. M., Yüzüak O., Aslan A.

Protein Journal, vol.41, no.6, pp.671-680, 2022 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 41 Issue: 6
  • Publication Date: 2022
  • Doi Number: 10.1007/s10930-022-10082-5
  • Journal Name: Protein Journal
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chemical Abstracts Core, EMBASE, MEDLINE, Veterinary Science Database
  • Page Numbers: pp.671-680
  • Keywords: Fe3O4, Glycidyl methacrylate, 5-Aminotetrazole, alpha-amylase, Immobilization
  • Kocaeli University Affiliated: No


© 2022, The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.Enzymes are a powerful tool employed in industrial applications due to their high specificity and efficiency. Amylase enzymes play an important role in detergent, textile, analytical chemistry, and paper industries. Here we present the design, synthesis, and characterization of azole functionalized nanoparticles for the immobilization of α-amylase from Bacillus licheniformis (BlA). A modest binding efficiency (47%) was determined by the BCA assay. Enzymatic activity was measured using DNS method and illustrated the immobilization of amylase with the designed nanoparticles enhanced the thermal stability and long-term storage of amylases at a wide range of temperatures and pHs. With the required scale-up study, these implications amplify novel ways to implement this Fe3O4-PGMA-5A immobilized BlA enzyme in particular industrial applications.