Literature DB >> 36266499

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

Sedef Kaptan Usul1, Barış Binay1, Ali Murat Soydan2, Okan Yüzüak3, Ayşe Aslan4.   

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.
© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

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

Year:  2022        PMID: 36266499     DOI: 10.1007/s10930-022-10082-5

Source DB:  PubMed          Journal:  Protein J        ISSN: 1572-3887            Impact factor:   4.000


  15 in total

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