Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis
An extracellular lipase partially purified from Bacillus thermoamylovorans BHK67 was effectively immobilized onto modified magnetic MgFe2O4 nanoparticles (NPs). NPs were prepared by the sol-gel auto-combustion method and characterized by Fourier transform infrared (FTIR) spectroscopy, X-ray diffract...
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doaj-bc7a126a940648e5b381791ce1905a752020-11-24T21:44:51ZengElsevierJournal of King Saud University: Science1018-36472017-10-0129453654610.1016/j.jksus.2017.08.005Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesisAbhishek Sharma0Anil Kumar1Khem Raj Meena2Shikha Rana3Mahavir Singh4Shamsher Singh Kanwar5Department of Biotechnology, Himachal Pradesh University, Shimla 171005, IndiaDepartment of Biotechnology, Himachal Pradesh University, Shimla 171005, IndiaDepartment of Biotechnology, Himachal Pradesh University, Shimla 171005, IndiaDepartment of Physics, Himachal Pradesh University, Shimla, HP 171005, IndiaDepartment of Physics, Himachal Pradesh University, Shimla, HP 171005, IndiaDepartment of Biotechnology, Himachal Pradesh University, Shimla 171005, IndiaAn extracellular lipase partially purified from Bacillus thermoamylovorans BHK67 was effectively immobilized onto modified magnetic MgFe2O4 nanoparticles (NPs). NPs were prepared by the sol-gel auto-combustion method and characterized by Fourier transform infrared (FTIR) spectroscopy, X-ray diffraction (XRD), Ultra-Violet–Visible Spectroscopy (UV–vis) and atomic force microscopy (AFM). Protein loading reached a saturated amount of about 0.20 mg lipase per milligram of MgFe2O4 NPs with 78.9% binding efficiency. The NPs-bound lipase also showed stability following exposure to n-propanol and iso-propanol or FeCl2 and MgCl2 metal ions at (1 mM) at 55 °C. NPs-bound lipase also retained 50% of its original hydrolytic activity even after 8th cycle, as well as after 12 h of incubation at 55 °C. NPs-bound lipase in an esterification reaction of n-propanol and gallic acid (25 mM) performed for 12 h at 55 °C produced n-propyl gallate with a conversion rate of 82%. Synthesized n-propyl gallate possessed strong antioxidant activity, which was confirmed by DPPH assay, and in addition has anticancerous activity which was tested on a human L132 cell line.http://www.sciencedirect.com/science/article/pii/S1018364717303968B. thermoamylovorans BHK67NPs-bound lipaseThermostabilityn-Propyl gallateEsterificationAntioxidant |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Abhishek Sharma Anil Kumar Khem Raj Meena Shikha Rana Mahavir Singh Shamsher Singh Kanwar |
spellingShingle |
Abhishek Sharma Anil Kumar Khem Raj Meena Shikha Rana Mahavir Singh Shamsher Singh Kanwar Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis Journal of King Saud University: Science B. thermoamylovorans BHK67 NPs-bound lipase Thermostability n-Propyl gallate Esterification Antioxidant |
author_facet |
Abhishek Sharma Anil Kumar Khem Raj Meena Shikha Rana Mahavir Singh Shamsher Singh Kanwar |
author_sort |
Abhishek Sharma |
title |
Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis |
title_short |
Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis |
title_full |
Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis |
title_fullStr |
Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis |
title_full_unstemmed |
Fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis |
title_sort |
fabrication and functionalization of magnesium nanoparticle for lipase immobilization in n-propyl gallate synthesis |
publisher |
Elsevier |
series |
Journal of King Saud University: Science |
issn |
1018-3647 |
publishDate |
2017-10-01 |
description |
An extracellular lipase partially purified from Bacillus thermoamylovorans BHK67 was effectively immobilized onto modified magnetic MgFe2O4 nanoparticles (NPs). NPs were prepared by the sol-gel auto-combustion method and characterized by Fourier transform infrared (FTIR) spectroscopy, X-ray diffraction (XRD), Ultra-Violet–Visible Spectroscopy (UV–vis) and atomic force microscopy (AFM). Protein loading reached a saturated amount of about 0.20 mg lipase per milligram of MgFe2O4 NPs with 78.9% binding efficiency. The NPs-bound lipase also showed stability following exposure to n-propanol and iso-propanol or FeCl2 and MgCl2 metal ions at (1 mM) at 55 °C. NPs-bound lipase also retained 50% of its original hydrolytic activity even after 8th cycle, as well as after 12 h of incubation at 55 °C. NPs-bound lipase in an esterification reaction of n-propanol and gallic acid (25 mM) performed for 12 h at 55 °C produced n-propyl gallate with a conversion rate of 82%. Synthesized n-propyl gallate possessed strong antioxidant activity, which was confirmed by DPPH assay, and in addition has anticancerous activity which was tested on a human L132 cell line. |
topic |
B. thermoamylovorans BHK67 NPs-bound lipase Thermostability n-Propyl gallate Esterification Antioxidant |
url |
http://www.sciencedirect.com/science/article/pii/S1018364717303968 |
work_keys_str_mv |
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