The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
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
Abstract
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 ~10 nm catalase molecules are embedded in 2 μm single-crystalline ZIF-90 crystals with ~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.
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Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Exceptional chemical and thermal stability of zeolitic imidazolate frameworks
Park, K. S., Ni, Z., Côté, A. P., Choi, J. Y., Huang, R., Uribe-Romo, F. J., Chae, H. K., O’Keeffe, M., & Yaghi, O. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602439103 · Cited by 7,563
High-Throughput Synthesis of Zeolitic Imidazolate Frameworks and Application to CO 2 Capture
Banerjee, R., Phan, A., Wang, B., Knobler, C., Furukawa, H., O'Keeffe, M., & Yaghi, O. M. (2008) · Science · doi:10.1126/science.1152516 · Cited by 4,205
Antioxidants, Oxidative Damage and Oxygen Deprivation Stress: a Review
BLOKHINA, O. (2003) · Annals of Botany · doi:10.1093/aob/mcf118 · Cited by 4,002
Enzyme Immobilization: The Quest for Optimum Performance
Sheldon, R. A. (2007) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.200700082 · Cited by 2,077
Industrial enzyme applications
Kirk, O., Borchert, T. V., & Fuglsang, C. C. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00328-2 · Cited by 1,461
Understanding enzyme immobilisation
Hanefeld, U., Gardossi, L., & Magner, E. (2009) · Chem. Soc. Rev. · doi:10.1039/b711564b · Cited by 1,237
One-Pot Synthesis of Protein-Embedded Metal–Organic Frameworks with Enhanced Biological Activities
Lyu, F., Zhang, Y., Zare, R. N., Ge, J., & Liu, Z. (2014) · Nano Letters · doi:10.1021/nl5026419 · Cited by 999
Zhuang, J., Kuo, C.-H., Chou, L.-Y., Liu, D.-Y., Weerapana, E., & Tsung, C.-K. (2014) · ACS Nano · doi:10.1021/nn406590q · Cited by 873
Self-citationMesoporous Silica Nanoparticles for Intracellular Delivery of Membrane-Impermeable Proteins
Slowing, I. I., Trewyn, B. G., & Lin, V. S.-Y. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0719780 · Cited by 795
Crystals as Molecules: Postsynthesis Covalent Functionalization of Zeolitic Imidazolate Frameworks
Morris, W., Doonan, C. J., Furukawa, H., Banerjee, R., & Yaghi, O. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805222x · Cited by 779
Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.
Deisseroth, A., & Dounce, A. L. (1970) · Physiological Reviews · doi:10.1152/physrev.1970.50.3.319 · Cited by 681
Proteins in Mesoporous Silicates
Hudson, S., Cooney, J., & Magner, E. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705238 · Cited by 663
Lykourinou, V., Chen, Y., Wang, X.-S., Meng, L., Hoang, T., Ming, L.-J., Musselman, R. L., & Ma, S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2038003 · Cited by 658
Polymeric protein delivery systems
Lee, K. Y., & Yuk, S. H. (2007) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2007.04.001 · Cited by 425
Chen, Y., Lykourinou, V., Vetromile, C., Hoang, T., Ming, L.-J., Larsen, R. W., & Ma, S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305144x · Cited by 367
Core–Shell Catalysts of Metal Nanoparticle Core and Metal–Organic Framework Shell
Hu, P., Morabito, J. V., & Tsung, C.-K. (2014) · ACS Catalysis · doi:10.1021/cs5012662 · Cited by 358
Self-citationMesoporous Silicate Sequestration and Release of Proteins
Han, Y.-J., Stucky, G. D., & Butler, A. (1999) · Journal of the American Chemical Society · doi:10.1021/ja992138r · Cited by 351
Nelson, J. M., & Griffin, E. G. (1916) · Journal of the American Chemical Society · doi:10.1021/ja02262a018 · Cited by 300
Trypsin and Papain Covalently Coupled to Porous Glass: Preparation and Characterization
Weetall, H. H. (1969) · Science · doi:10.1126/science.166.3905.615 · Cited by 244
Shieh, F., Wang, S., Leo, S., & Wu, K. C. ‐. (2013) · Chemistry – A European Journal · doi:10.1002/chem.201301560 · Cited by 203
Self-citationRNA‐Directed Packaging of Enzymes within Virus‐like Particles
Fiedler, J. D., Brown, S. D., Lau, J. L., & Finn, M. G. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201005243 · Cited by 201
Ou, P., & Wolff, S. P. (1996) · Journal of Biochemical and Biophysical Methods · doi:10.1016/0165-022x(95)00039-t · Cited by 153
Osathanon, T., Giachelli, C. M., & Somerman, M. J. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.05.022 · Cited by 143
Enzymatic Cascade Reactions inside Polymeric Nanocontainers: A Means to Combat Oxidative Stress
Tanner, P., Onaca, O., Balasubramanian, V., Meier, W. P., & Palivan, C. G. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002782 · Cited by 136
Research and application of biotechnology in textile industries in China
Chen, J., Wang, Q., Hua, Z., & Du, G. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.07.040 · Cited by 99
A Nanoporous Reactor for Efficient Proteolysis
Qiao, L., Liu, Y., Hudson, S. P., et al. (2007) · Chemistry - A European Journal · doi:10.1002/chem.200701102 · Cited by 81
Nakashima, K., Kamiya, N., Koda, D., Maruyama, T., & Goto, M. (2009) · Organic & Biomolecular Chemistry · doi:10.1039/b823064a · Cited by 56
Steady-State Kinetics of the Catalase Reaction in the Presence of Cyanide
OGURA, Y., & Yamazaki, I. (1983) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a134369 · Cited by 44
Adsorption and Activity of a Domoic Acid Binding Antibody Fragment on Mesoporous Silicates
Hu, X., Spada, S., White, S. J., Hudson, S. P., Magner, E., & Wall, J. G. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp062423e · Cited by 33
Cited by
Metal–organic frameworks meet metal nanoparticles: synergistic effect for enhanced catalysis
Yang, Q., Xu, Q., & Jiang, H.-L. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00724d · Cited by 1,892
Hydrogen-Bonded Organic Frameworks as a Tunable Platform for Functional Materials
Wang, B., Lin, R.-B., Zhang, Z., Xiang, S., & Chen, B. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c06473 · Cited by 852
Metal–Organic Framework-Based Enzyme Biocomposites
Liang, W., Wied, P., Carraro, F., Sumby, C. J., Nidetzky, B., Tsung, C.-K., Falcaro, P., & Doonan, C. J. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01029 · Cited by 784
Self-citationEnhanced Activity of Enzymes Encapsulated in Hydrophilic Metal–Organic Frameworks
Liang, W., Xu, H., Carraro, F., Maddigan, N. K., Li, Q., Bell, S. G., Huang, D. M., Tarzia, A., Solomon, M. B., Amenitsch, H., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10302 · Cited by 560
Alsaiari, S. K., Patil, S., Alyami, M., Alamoudi, K. O., Aleisa, F. A., Merzaban, J. S., Li, M., & Khashab, N. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.7b11754 · Cited by 517
Metadata
- Authors
- Shieh, F.-K., Wang, S.-C., Yen, C.-I., Wu, C.-C., Dutta, S., Chou, L.-Y., Morabito, J. V., Hu, P., Hsu, M.-H., Wu, K. C.-W., & Tsung, C.-K.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-03-27
- Volume
- 137
- Issue
- 13
- Pages
- 4276-4279
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2331326812
- Cited by
- 774
- References
- 30
- FWCI
- 28.56
- Type
- journal article
- Language
- en
- Open access
- closed
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