Utility of Silane-Modified Magnesium-Based Magnetic Nanoparticles for Efficient Immobilization of Bacillus thermoamylovorans Lipase
Enzymes and protein's immobilization on magnetic nano supports is emerging as a promising candidate in the food, medical field, and areas of environmental studies. This work presents a study on purified Bacillus thermoamylovorans lipase (BTL) by utilizing tetraethoxysilane (TEOS)-modified magnesium nano ferrite (MgNF) of 20 nm size. Its structural and morphological studies were investigated by powder X-ray diffractometry, high-resolution transmission electron microscopy, etc. Binding of BTL with MgNF was supported by using Fourier transform infrared spectroscopy. Magnetic behavior was examined by the vibrational sample magnetometer and Mössbauer spectrometer graphs. The enzymatic activity of BTL before and after immobilization was studied at different temperatures and reaction time. As per the Lineweaver-Burk plot, immobilized lipase has more biological affinity for fatty acids in comparison to the free lipase, and Kmax values of immobilized and free BTL were computed as 6.6 and 7.5 mM respectively, with excellent reusability(> 50%) even till 13 consecutive assay runs. Graphical Abstract.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:192 |
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| Enthalten in: |
Applied biochemistry and biotechnology - 192(2020), 3 vom: 08. Nov., Seite 1029-1043 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Rana, Shikha [VerfasserIn] |
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| Links: |
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| Themen: |
EC 3.1.1.3 |
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| Anmerkungen: |
Date Completed 20.05.2021 Date Revised 20.05.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1007/s12010-020-03379-7 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM312156898 |
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| 520 | |a Enzymes and protein's immobilization on magnetic nano supports is emerging as a promising candidate in the food, medical field, and areas of environmental studies. This work presents a study on purified Bacillus thermoamylovorans lipase (BTL) by utilizing tetraethoxysilane (TEOS)-modified magnesium nano ferrite (MgNF) of 20 nm size. Its structural and morphological studies were investigated by powder X-ray diffractometry, high-resolution transmission electron microscopy, etc. Binding of BTL with MgNF was supported by using Fourier transform infrared spectroscopy. Magnetic behavior was examined by the vibrational sample magnetometer and Mössbauer spectrometer graphs. The enzymatic activity of BTL before and after immobilization was studied at different temperatures and reaction time. As per the Lineweaver-Burk plot, immobilized lipase has more biological affinity for fatty acids in comparison to the free lipase, and Kmax values of immobilized and free BTL were computed as 6.6 and 7.5 mM respectively, with excellent reusability(> 50%) even till 13 consecutive assay runs. Graphical Abstract | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Immobilization | |
| 650 | 4 | |a Magnesium nanoferrite | |
| 650 | 4 | |a Mössbauer | |
| 650 | 4 | |a Reusability | |
| 650 | 4 | |a Silane | |
| 650 | 7 | |a Enzymes, Immobilized |2 NLM | |
| 650 | 7 | |a Fatty Acids |2 NLM | |
| 650 | 7 | |a Silanes |2 NLM | |
| 650 | 7 | |a Lipase |2 NLM | |
| 650 | 7 | |a EC 3.1.1.3 |2 NLM | |
| 650 | 7 | |a Magnesium |2 NLM | |
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| 700 | 1 | |a Sharma, Abhishek |e verfasserin |4 aut | |
| 700 | 1 | |a Kumar, Arun |e verfasserin |4 aut | |
| 700 | 1 | |a Kanwar, Shamsher Singh |e verfasserin |4 aut | |
| 700 | 1 | |a Singh, Mahavir |e verfasserin |4 aut | |
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