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Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles

The current research demonstrates the synthesis of zinc oxide nanoparticles (ZnO-NPs) via green nanotechnology approach (Azatirachta indica leaves). The size of the synthesized ZnO-NPs was confirmed as 27 nm by TEM. Glutaraldehyde was used to modify the surface of the developed ZnO-NPs in order to p...

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Detalles Bibliográficos
Autores principales: Ansari, Shakeel Ahmed, Damanhory, Ahmed Abdelghany
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9898663/
https://www.ncbi.nlm.nih.gov/pubmed/36747522
http://dx.doi.org/10.1016/j.heliyon.2023.e13089
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author Ansari, Shakeel Ahmed
Damanhory, Ahmed Abdelghany
author_facet Ansari, Shakeel Ahmed
Damanhory, Ahmed Abdelghany
author_sort Ansari, Shakeel Ahmed
collection PubMed
description The current research demonstrates the synthesis of zinc oxide nanoparticles (ZnO-NPs) via green nanotechnology approach (Azatirachta indica leaves). The size of the synthesized ZnO-NPs was confirmed as 27 nm by TEM. Glutaraldehyde was used to modify the surface of the developed ZnO-NPs in order to promote covalent binding of Aspergillus oryzae β-galactosidase. Enzyme activity was achieved as 93% on glutaraldehyde modified ZnO-NPs. The immobilized enzyme exhibited significant enhancement in activity under extreme temperature and pH variations, as compared to the soluble β-galactosidase (SβG). It was further observed that the immobilized enzyme retained 58% activity at 5% galactose concentration. However, under similar experimental conditions, SβG showed 27% activity. Reusability of immobilized enzyme revealed that it retained 89% activity even after fifth repeated use, and hence could be recovered easily by centrifugation for repeated use in biotechnological applications. Batch reactor experiment indicates that the immobilized enzyme displayed 81% and 70% lactose hydrolysis at 50 °C and 60 °C, respectively as compared to 70% and 58% lactose hydrolysis by soluble enzyme under identical conditions after 9 h.
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spelling pubmed-98986632023-02-05 Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles Ansari, Shakeel Ahmed Damanhory, Ahmed Abdelghany Heliyon Research Article The current research demonstrates the synthesis of zinc oxide nanoparticles (ZnO-NPs) via green nanotechnology approach (Azatirachta indica leaves). The size of the synthesized ZnO-NPs was confirmed as 27 nm by TEM. Glutaraldehyde was used to modify the surface of the developed ZnO-NPs in order to promote covalent binding of Aspergillus oryzae β-galactosidase. Enzyme activity was achieved as 93% on glutaraldehyde modified ZnO-NPs. The immobilized enzyme exhibited significant enhancement in activity under extreme temperature and pH variations, as compared to the soluble β-galactosidase (SβG). It was further observed that the immobilized enzyme retained 58% activity at 5% galactose concentration. However, under similar experimental conditions, SβG showed 27% activity. Reusability of immobilized enzyme revealed that it retained 89% activity even after fifth repeated use, and hence could be recovered easily by centrifugation for repeated use in biotechnological applications. Batch reactor experiment indicates that the immobilized enzyme displayed 81% and 70% lactose hydrolysis at 50 °C and 60 °C, respectively as compared to 70% and 58% lactose hydrolysis by soluble enzyme under identical conditions after 9 h. Elsevier 2023-01-23 /pmc/articles/PMC9898663/ /pubmed/36747522 http://dx.doi.org/10.1016/j.heliyon.2023.e13089 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Ansari, Shakeel Ahmed
Damanhory, Ahmed Abdelghany
Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
title Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
title_full Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
title_fullStr Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
title_full_unstemmed Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
title_short Biotechnological application of Aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
title_sort biotechnological application of aspergillus oryzae β-galactosidase immobilized on glutaraldehyde modified zinc oxide nanoparticles
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9898663/
https://www.ncbi.nlm.nih.gov/pubmed/36747522
http://dx.doi.org/10.1016/j.heliyon.2023.e13089
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