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Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal

Lipase was immobilized onto bacterial magnetosomes using glutaraldehyde cross-linking and confirmed by Fourier transform infrared spectrometry (FT-IR) and Scanning electron microscopy (SEM). Enzyme activity of immobilised lipase as well as free lipase was estimated by the release of p-nitro phenol d...

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Autores principales: Jacob, Jobin John, Suthindhiran, K
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6976927/
https://www.ncbi.nlm.nih.gov/pubmed/31993344
http://dx.doi.org/10.1016/j.btre.2020.e00422
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author Jacob, Jobin John
Suthindhiran, K
author_facet Jacob, Jobin John
Suthindhiran, K
author_sort Jacob, Jobin John
collection PubMed
description Lipase was immobilized onto bacterial magnetosomes using glutaraldehyde cross-linking and confirmed by Fourier transform infrared spectrometry (FT-IR) and Scanning electron microscopy (SEM). Enzyme activity of immobilised lipase as well as free lipase was estimated by the release of p-nitro phenol due to the hydrolysis of p-nitro phenyl acetate (pNPA). The immobilisation yield of lipase onto magnetosome was found to be 88 %. The optimal pH (7) and temperature (40 °C) for activity was standardised and found to be similar to free lipase. The stored immobilized lipase maintained higher activity even after 30 days at a temperature of 4 °C whereas compared to free lipase. Immobilized lipase found to have removed vegetable oil stain and showed higher cleaning efficiency when compared to free lipase. The results suggest that bacterial magnetosome displays great potential as a support material for the immobilization of industrial enzymes such as lipase.
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spelling pubmed-69769272020-01-28 Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal Jacob, Jobin John Suthindhiran, K Biotechnol Rep (Amst) Research Article Lipase was immobilized onto bacterial magnetosomes using glutaraldehyde cross-linking and confirmed by Fourier transform infrared spectrometry (FT-IR) and Scanning electron microscopy (SEM). Enzyme activity of immobilised lipase as well as free lipase was estimated by the release of p-nitro phenol due to the hydrolysis of p-nitro phenyl acetate (pNPA). The immobilisation yield of lipase onto magnetosome was found to be 88 %. The optimal pH (7) and temperature (40 °C) for activity was standardised and found to be similar to free lipase. The stored immobilized lipase maintained higher activity even after 30 days at a temperature of 4 °C whereas compared to free lipase. Immobilized lipase found to have removed vegetable oil stain and showed higher cleaning efficiency when compared to free lipase. The results suggest that bacterial magnetosome displays great potential as a support material for the immobilization of industrial enzymes such as lipase. Elsevier 2020-01-17 /pmc/articles/PMC6976927/ /pubmed/31993344 http://dx.doi.org/10.1016/j.btre.2020.e00422 Text en © 2020 Published by Elsevier B.V. http://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
Jacob, Jobin John
Suthindhiran, K
Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
title Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
title_full Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
title_fullStr Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
title_full_unstemmed Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
title_short Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
title_sort immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6976927/
https://www.ncbi.nlm.nih.gov/pubmed/31993344
http://dx.doi.org/10.1016/j.btre.2020.e00422
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