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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2023
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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. |
format | Online Article Text |
id | pubmed-9898663 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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