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Protein-inorganic hybrid nanoflowers
文献类型：期刊论文
| 作者 | Ge, Jun1,3; Lei, Jiandu2,3; Zare, Richard N.3 |
| 刊名 | NATURE NANOTECHNOLOGY
 |
| 出版日期 | 2012-07-01 |
| 卷号 | 7期号:7页码:428-432 |
| 关键词 | single-enzyme metal-ions nanogel immobilization nanostructures nanodendrites resolution support binding laccase |
| ISSN号 | 1748-3387 |
| 其他题名 | Nat. Nanotechnol. |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology ; Technology |
| 类目[WOS] | Nanoscience & Nanotechnology ; Materials Science, Multidisciplinary |
| 研究领域[WOS] | Science & Technology - Other Topics ; Materials Science |
| 关键词[WOS] | SINGLE-ENZYME ; METAL-IONS ; NANOGEL ; IMMOBILIZATION ; NANOSTRUCTURES ; NANODENDRITES ; RESOLUTION ; SUPPORT ; BINDING ; LACCASE |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000306112000008 |
| 公开日期 | 2013-11-28 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/6460]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 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 |
| 推荐引用方式 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. |
入库方式： OAI收割
来源：过程工程研究所
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