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. 2022 Dec;41(6):671-680.
doi: 10.1007/s10930-022-10082-5. Epub 2022 Oct 20.

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

Sedef Kaptan Usul  1 , Barış Binay  1 , Ali Murat Soydan  2 , Okan Yüzüak  3 , Ayşe Aslan  4
Affiliations

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

Sedef Kaptan Usul et al. Protein J. 2022 Dec.

Abstract

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.

Keywords: 5-Aminotetrazole; Fe3O4; Glycidyl methacrylate; Immobilization; α-amylase.

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