Stable metal-organic frameworks containing single-molecule traps for enzyme encapsulation

Dawei Feng, Tian-Fu Liu, Jie Su, Mathieu Bosch, Zhangwen Wei, Wei Wan, Daqiang Yuan, Ying-Pin Chen, Xuan Wang, Kecheng Wang, Xizhen Lian, Zhi-Yuan Gu, Jihye Park, Xiaodong Zou and Hong-Cai Zhou ()
Additional contact information
Dawei Feng: Texas A&M University
Tian-Fu Liu: Texas A&M University
Jie Su: Berzelii Centre EXSELENT on Porous Materials and Inorganic and Structural Chemistry, Stockholm University
Mathieu Bosch: Texas A&M University
Zhangwen Wei: Texas A&M University
Wei Wan: Berzelii Centre EXSELENT on Porous Materials and Inorganic and Structural Chemistry, Stockholm University
Daqiang Yuan: State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fujian
Ying-Pin Chen: Texas A&M University
Xuan Wang: Texas A&M University
Kecheng Wang: Texas A&M University
Xizhen Lian: Texas A&M University
Zhi-Yuan Gu: Texas A&M University
Jihye Park: Texas A&M University
Xiaodong Zou: Berzelii Centre EXSELENT on Porous Materials and Inorganic and Structural Chemistry, Stockholm University
Hong-Cai Zhou: Texas A&M University

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract Enzymatic catalytic processes possess great potential in chemical manufacturing, including pharmaceuticals, fuel production and food processing. However, the engineering of enzymes is severely hampered due to their low operational stability and difficulty of reuse. Here, we develop a series of stable metal-organic frameworks with rationally designed ultra-large mesoporous cages as single-molecule traps (SMTs) for enzyme encapsulation. With a high concentration of mesoporous cages as SMTs, PCN-333(Al) encapsulates three enzymes with record-high loadings and recyclability. Immobilized enzymes that most likely undergo single-enzyme encapsulation (SEE) show smaller Km than free enzymes while maintaining comparable catalytic efficiency. Under harsh conditions, the enzyme in SEE exhibits better performance than free enzyme, showing the effectiveness of SEE in preventing enzyme aggregation or denaturation. With extraordinarily large pore size and excellent chemical stability, PCN-333 may be of interest not only for enzyme encapsulation, but also for entrapment of other nanoscaled functional moieties.

Date: 2015
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DOI: 10.1038/ncomms6979

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