Imparting Functionality to Biocatalysts via Embedding Enzymes into Nanoporous Materials by a de Novo Approach: Size-Selective Sheltering of Catalase in Metal-Organic Framework Microcrystals

被引:794
作者
Shieh, Fa-Kuen [1 ]
Wang, Shao-Chun [1 ]
Yen, Chia-I [1 ]
Wu, Chang-Cheng [1 ]
Dutta, Saikat [2 ]
Chou, Lien-Yan [3 ]
Morabito, Joseph V. [3 ]
Hu, Pan [3 ]
Hsu, Ming-Hua [4 ]
Wu, Kevin C. -W. [2 ]
Tsung, Chia-Kuang [3 ]
机构
[1] Natl Cent Univ, Dept Chem, Chungli 32001, Taiwan
[2] Natl Taiwan Univ, Dept Chem Engn, Taipei 10617, Taiwan
[3] Boston Coll, Dept Chem, Merkert Chem Ctr, Chestnut Hill, MA 02467 USA
[4] Natl Tsing Hua Univ, Nucl Sci & Technol Dev Ctr, Hsinchu 30013, Taiwan
关键词
ZEOLITIC IMIDAZOLATE FRAMEWORKS; MESOPOROUS SILICATES; PROTEINS; IMMOBILIZATION; DELIVERY; ADSORPTION; CATALYSIS; MOLECULE; BINDING; MOF;
D O I
10.1021/ja513058h
中图分类号
O6 [化学];
学科分类号
070301 [无机化学];
摘要
We develop a new concept to impart new functions to biocatalysts by combining enzymes and metal-organic frameworks (MOFs). The proof-of-concept design is demonstrated by embedding catalase molecules into uniformly sized ZIF-90 crystals via a de novo approach. We have carried out electron microscopy, X-ray diffraction, nitrogen sorption, electrophoresis, thermogravimetric analysis, and confocal microscopy to confirm that the similar to 10 nm catalase molecules are embedded in 2 mu m single-crystalline ZIF-90 crystals with similar to 5 wt % loading. Because catalase is immobilized and sheltered by the ZIF-90 crystals, the composites show activity in hydrogen peroxide degradation even in the presence of protease proteinase K.
引用
收藏
页码:4276 / 4279
页数:4
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