Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles
This work presents the synthesis and use of surface-modified iron oxide nanoparticles for the covalent immobilization of Bacillus licheniformis γ-glutamyl transpeptidase (BlGGT). Magnetic nanoparticles were prepared by an alkaline solution of divalent and trivalent iron ions, and they were subsequen...
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| Format: | Article |
| Language: | English |
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MDPI AG
2013-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | http://www.mdpi.com/1422-0067/14/3/4613 |
| _version_ | 1811334802603769856 |
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| author | Meng-Chun Chi Long-Liu Lin Tzu-Fan Wang Yi-Yu Chen Ming-Gen Tsai |
| author_facet | Meng-Chun Chi Long-Liu Lin Tzu-Fan Wang Yi-Yu Chen Ming-Gen Tsai |
| author_sort | Meng-Chun Chi |
| collection | DOAJ |
| description | This work presents the synthesis and use of surface-modified iron oxide nanoparticles for the covalent immobilization of Bacillus licheniformis γ-glutamyl transpeptidase (BlGGT). Magnetic nanoparticles were prepared by an alkaline solution of divalent and trivalent iron ions, and they were subsequently treated with 3-aminopropyltriethoxysilane (APES) to obtain the aminosilane-coated nanoparticles. The functional group on the particle surface and the amino group of BlGGT was then cross-linked using glutaraldehyde as the coupling reagent. The loading capacity of the prepared nanoparticles for BlGGT was 34.2 mg/g support, corresponding to 52.4% recovery of the initial activity. Monographs of transmission electron microscopy revealed that the synthesized nanoparticles had a mean diameter of 15.1 ± 3.7 nm, and the covalent cross-linking of the enzyme did not significantly change their particle size. Fourier transform infrared spectroscopy confirmed the immobilization of BlGGT on the magnetic nanoparticles. The chemical and kinetic behaviors of immobilized BlGGT are mostly consistent with those of the free enzyme. The immobilized enzyme could be recycled ten times with 36.2% retention of the initial activity and had a comparable stability respective to free enzyme during the storage period of 30 days. Collectively, the straightforward synthesis of aldehyde-functionalized nanoparticles and the efficiency of enzyme immobilization offer wide perspectives for the practical use of surface-bound BlGGT. |
| first_indexed | 2024-04-13T17:13:43Z |
| format | Article |
| id | doaj.art-3769809b5c924e24b2a155c11b1d35ac |
| institution | Directory Open Access Journal |
| issn | 1422-0067 |
| language | English |
| last_indexed | 2024-04-13T17:13:43Z |
| publishDate | 2013-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-3769809b5c924e24b2a155c11b1d35ac2022-12-22T02:38:11ZengMDPI AGInternational Journal of Molecular Sciences1422-00672013-02-011434613462810.3390/ijms14034613Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic NanoparticlesMeng-Chun ChiLong-Liu LinTzu-Fan WangYi-Yu ChenMing-Gen TsaiThis work presents the synthesis and use of surface-modified iron oxide nanoparticles for the covalent immobilization of Bacillus licheniformis γ-glutamyl transpeptidase (BlGGT). Magnetic nanoparticles were prepared by an alkaline solution of divalent and trivalent iron ions, and they were subsequently treated with 3-aminopropyltriethoxysilane (APES) to obtain the aminosilane-coated nanoparticles. The functional group on the particle surface and the amino group of BlGGT was then cross-linked using glutaraldehyde as the coupling reagent. The loading capacity of the prepared nanoparticles for BlGGT was 34.2 mg/g support, corresponding to 52.4% recovery of the initial activity. Monographs of transmission electron microscopy revealed that the synthesized nanoparticles had a mean diameter of 15.1 ± 3.7 nm, and the covalent cross-linking of the enzyme did not significantly change their particle size. Fourier transform infrared spectroscopy confirmed the immobilization of BlGGT on the magnetic nanoparticles. The chemical and kinetic behaviors of immobilized BlGGT are mostly consistent with those of the free enzyme. The immobilized enzyme could be recycled ten times with 36.2% retention of the initial activity and had a comparable stability respective to free enzyme during the storage period of 30 days. Collectively, the straightforward synthesis of aldehyde-functionalized nanoparticles and the efficiency of enzyme immobilization offer wide perspectives for the practical use of surface-bound BlGGT.http://www.mdpi.com/1422-0067/14/3/4613Bacillus licheniformisγ-glutamyl transpeptidasemagnetic nanoparticle3-aminopropyltriethoxysilanecovalent immobilization |
| spellingShingle | Meng-Chun Chi Long-Liu Lin Tzu-Fan Wang Yi-Yu Chen Ming-Gen Tsai Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles International Journal of Molecular Sciences Bacillus licheniformis γ-glutamyl transpeptidase magnetic nanoparticle 3-aminopropyltriethoxysilane covalent immobilization |
| title | Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles |
| title_full | Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles |
| title_fullStr | Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles |
| title_full_unstemmed | Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles |
| title_short | Covalent Immobilization of Bacillus licheniformis γ-Glutamyl Transpeptidase on Aldehyde-Functionalized Magnetic Nanoparticles |
| title_sort | covalent immobilization of bacillus licheniformis γ glutamyl transpeptidase on aldehyde functionalized magnetic nanoparticles |
| topic | Bacillus licheniformis γ-glutamyl transpeptidase magnetic nanoparticle 3-aminopropyltriethoxysilane covalent immobilization |
| url | http://www.mdpi.com/1422-0067/14/3/4613 |
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