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Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal
•Lipase was immobilized on magnetosome via glutaraldehyde, confirmed in FTIR and SEM.•Release of p-nitro phenol confirmed the enzyme activity of immobilize lipase (88 %).•The optimal pH (7) and temperature (40 °C) was standardised for activity.•The immobilized lipase stored at 4 °C retained higher a...
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Published in: | Biotechnology reports (Amsterdam, Netherlands) Netherlands), 2020-03, Vol.25, p.e00422-e00422, Article e00422 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •Lipase was immobilized on magnetosome via glutaraldehyde, confirmed in FTIR and SEM.•Release of p-nitro phenol confirmed the enzyme activity of immobilize lipase (88 %).•The optimal pH (7) and temperature (40 °C) was standardised for activity.•The immobilized lipase stored at 4 °C retained higher activity (87 %) than free lipase after 30 days.•Immobilized lipase removed vegetable oil stain, better cleaning efficiency than free lipase.
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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ISSN: | 2215-017X 2215-017X |
DOI: | 10.1016/j.btre.2020.e00422 |