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

Stable metal-organic frameworks containing single-molecule traps for enzyme encapsulation
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DOI:
10.1038/ncomms6979
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发表时间:
2015-01-01
影响因子:
16.6
通讯作者:
Zhou, Hong-Cai
Zhou, Hong-Cai
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Feng, Dawei;Liu, Tian-Fu;Zhou, Hong-Cai

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酶催化过程在化学制造中具有巨大的潜力,包括制药、燃料生产和食品加工。然而,由于酶的低操作稳定性和难以重复使用,严重阻碍了酶的工程化。在这里,我们开发了一系列稳定的金属有机框架,并合理设计了超大介孔笼作为酶包封的单分子陷阱(SMTs)。PCN-333(Al)采用高浓度的介孔笼作为smt,封装了三种酶,具有创纪录的高负荷和可回收性。固定化酶最有可能进行单酶包封(SEE),其Km比游离酶小,同时保持相当的催化效率。在恶劣条件下,SEE中的酶表现出比游离酶更好的性能,显示了SEE在防止酶聚集或变性方面的有效性。由于具有超大孔径和优异的化学稳定性,PCN-333不仅可以用于酶包封,还可以用于其他纳米级功能基团的包封。
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.