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

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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.

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Acknowledgements

The authors gratefully acknowledge GERC (Gebze Enzyme Recognition Center, Gebze Technical University Turkey) for the support and Hayat Kimya Corp. for providing the expression vector containing the amyS gene from Bacillus licheniformis. We also would like to thank Mehmet Mervan Çakar for his support in experimental studies (University of Zagreb, Croatia), Ahmet Nazım for SEM images, and Adem Şen for XRD (Materials Science and Engineering, Gebze Technical University Turkey).

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Authors and Affiliations

  1. Department of Bioengineering, Gebze Technical University, Kocaeli, Turkey

    Sedef Kaptan Usul, Barış Binay & Ayşe Aslan

  2. Institute of Energy Technologies, Gebze Technical University, Kocaeli, Turkey

    Ali Murat Soydan

  3. Hayat Kimya, İstanbul, Turkey

    Okan Yüzüak

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  1. Sedef Kaptan Usul
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  2. Barış Binay
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Kaptan Usul, S., Binay, B., Soydan, A.M. et al. Immobilization of the Bacillus licheniformis α-Amylase on Azole Functionalized Nanoparticle: More Active, Stable, and Usability. Protein J 41, 671–680 (2022). https://doi.org/10.1007/s10930-022-10082-5

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