Highly active enzyme-metal nanohybrids synthesized in protein-polymer conjugates
文献类型：期刊论文
| 作者 | Li, XY; Cao, YF; Luo, K; Sun, YZ; Xiong, JR; Wang, LC; Liu, Z; Li, J; Ma, JY; Ge, J |
| 刊名 | NATURE CATALYSIS
 |
| 出版日期 | 2019 |
| 卷号 | 2期号:8页码:718-725 |
| 关键词 | DYNAMIC KINETIC RESOLUTION TOTAL-ENERGY CALCULATIONS PRIMARY AMINES CHIRAL AMINES RACEMIZATION PD CATALYSTS PALLADIUM IMMOBILIZATION NANOPARTICLES |
| ISSN号 | 2520-1158 |
| DOI | 10.1038/s41929-019-0305-8 |
| 文献子类 | 期刊论文 |
| 英文摘要 | Building a bridge between enzymatic and heterogeneous catalysis provides new cascade industrial processes for manufacturing. However, the reaction conditions of enzymatic and heterogeneous catalysis mutually cause deactivation of catalysts. Here, we overcame this challenge by developing a special protocol for the synthesis of hybrid catalysts. We utilized protein-polymer nanoconjugates as confined nanoreactors for the in situ synthesis of lipase-palladium (Pd) nanohybrids. The 0.8 nm Pd nanoparticles exhibited increased activity in racemization of (S)-1-phenylethylamine. At 55 degrees C, which matches the optimum temperature of lipase, the activity is more than 50 times that of commercial Pd/C. It was found that the Pd-O coordination in Pd subnanoclusters contributed to the high activity. In the dynamic kinetic resolutions of pharmaceutical intermediates (+/-)-1-phenylethylamine, (+/-)-1-aminoindan and (+/-)-1,2,3,4-tetrahydro-1-naphthylamine, the lipase-Pd nanohybrids displayed 7.6, 3.1 and 5.0 times higher efficiencies than the combination of commercial immobilized lipase Novozym 435 and Pd/C. The lipase-Pd nanohybrids can be reused without agglomeration and activity loss. |
| 语种 | 英语 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/32082]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 作者单位 | 1.Tsinghua Univ, Dept Chem Engn, Key Lab Ind Biocatalysis, Minist Educ, Beijing, Peoples R China; 2.Fudan Univ, Dept Chem, Jiangwan Campus, Shanghai, Peoples R China; 3.Tsinghua Univ, Dept Chem, Beijing, Peoples R China; 4.Chinese Acad Sci, Shanghai Inst Appl Phys, Shanghai Synchrotron Radiat Facil, Shanghai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, XY,Cao, YF,Luo, K,et al. Highly active enzyme-metal nanohybrids synthesized in protein-polymer conjugates[J]. NATURE CATALYSIS,2019,2(8):718-725. |
| APA | Li, XY.,Cao, YF.,Luo, K.,Sun, YZ.,Xiong, JR.,...&Zare, RN.(2019).Highly active enzyme-metal nanohybrids synthesized in protein-polymer conjugates.NATURE CATALYSIS,2(8),718-725. |
| MLA | Li, XY,et al."Highly active enzyme-metal nanohybrids synthesized in protein-polymer conjugates".NATURE CATALYSIS 2.8(2019):718-725. |
入库方式： OAI收割
来源：上海应用物理研究所
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