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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Main Authors: Abhishek Sharma, Anil Kumar, Khem Raj Meena, Shikha Rana, Mahavir Singh, Shamsher Singh Kanwar
Format: Article
Language:English
Published: Elsevier 2017-10-01
Series:Journal of King Saud University: Science
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S1018364717303968
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spelling 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
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