Knowledge Management System Of Institute of process engineering,CAS
| Protein-inorganic hybrid nanoflowers | |
| Alternative Title | Nat. Nanotechnol. |
| Ge, Jun1,3; Lei, Jiandu2,3; Zare, Richard N.3 | |
| 2012-07-01 | |
| Source Publication | NATURE NANOTECHNOLOGY
 |
| ISSN | 1748-3387 |
| Volume | 7Issue:7Pages:428-432 |
| Abstract | Flower-shaped inorganic nanocrystals(1-3) have been used for applications in catalysis(4,5) and analytical science(6,7), but so far there have been no reports of 'nanoflowers' made of organic components(8). Here, we report a method for creating hybrid organic-inorganic nanoflowers using copper (II) ions as the inorganic component and various proteins as the organic component. The protein molecules form complexes with the copper ions, and these complexes become nucleation sites for primary crystals of copper phosphate. Interaction between the protein and copper ions then leads to the growth of micrometre-sized particles that have nanoscale features and that are shaped like flower petals. When an enzyme is used as the protein component of the hybrid nanoflower, it exhibits enhanced enzymatic activity and stability compared with the free enzyme. This is attributed to the high surface area and confinement of the enzymes in the nanoflowers.; Flower-shaped inorganic nanocrystals(1-3) have been used for applications in catalysis(4,5) and analytical science(6,7), but so far there have been no reports of 'nanoflowers' made of organic components(8). Here, we report a method for creating hybrid organic-inorganic nanoflowers using copper (II) ions as the inorganic component and various proteins as the organic component. The protein molecules form complexes with the copper ions, and these complexes become nucleation sites for primary crystals of copper phosphate. Interaction between the protein and copper ions then leads to the growth of micrometre-sized particles that have nanoscale features and that are shaped like flower petals. When an enzyme is used as the protein component of the hybrid nanoflower, it exhibits enhanced enzymatic activity and stability compared with the free enzyme. This is attributed to the high surface area and confinement of the enzymes in the nanoflowers. |
| Keyword | Single-enzyme Metal-ions Nanogel Immobilization Nanostructures Nanodendrites Resolution Support Binding Laccase |
| Subtype | Article |
| WOS Headings | Science & Technology ; Technology |
| DOI | 10.1038/NNANO.2012.80 |
| URL | 查看原文 |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | SINGLE-ENZYME ; METAL-IONS ; NANOGEL ; IMMOBILIZATION ; NANOSTRUCTURES ; NANODENDRITES ; RESOLUTION ; SUPPORT ; BINDING ; LACCASE |
| WOS Research Area | Science & Technology - Other Topics ; Materials Science |
| WOS Subject | Nanoscience & Nanotechnology ; Materials Science, Multidisciplinary |
| WOS ID | WOS:000306112000008 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Version | 出版稿 |
| Identifier | http://ir.ipe.ac.cn/handle/122111/6460 |
| Collection | 研究所（批量导入） |
| Affiliation | 1.Tsinghua Univ, Dept Chem Engn, Beijing 100084, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 3.Stanford Univ, Dept Chem, Stanford, CA 94305 USA |
| Recommended Citation GB/T 7714 | Ge, Jun,Lei, Jiandu,Zare, Richard N.. Protein-inorganic hybrid nanoflowers[J]. NATURE NANOTECHNOLOGY,2012,7(7):428-432. |
| APA | Ge, Jun,Lei, Jiandu,&Zare, Richard N..(2012).Protein-inorganic hybrid nanoflowers.NATURE NANOTECHNOLOGY,7(7),428-432. |
| MLA | Ge, Jun,et al."Protein-inorganic hybrid nanoflowers".NATURE NANOTECHNOLOGY 7.7(2012):428-432. |
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| Protein–inorganic hy（4055KB） | 限制开放 | CC BY-NC-SA | Application Full Text | |||
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