Assessment of Enzyme Functionality at Metal-Organic Framework Interfaces Developed through Molecular Simulations
Assessment of Enzyme Functionality at Metal-Organic Framework Interfaces Developed through Molecular Simulations
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DOI：
10.1021/acs.langmuir.2c02347
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发表时间：
2023-01-24
期刊：
影响因子：
3.9
通讯作者：
Dinu, Cerasela Zoica
中科院分区：
文献类型：
--
作者：
Chapman, Jordan;Dinu, Cerasela Zoica
酶将底物转化为产物的催化效率和无与伦比的选择性已被用于生物医学技术、生物燃料生产、气体传感和商品化学品升级等领域的广泛化学转化。然而，由于高温和工业溶剂存在下不可逆的生物催化剂变性，缺乏可重复使用性和天然催化活性的损失，酶实施的可行性受到挑战。酶固定化是酶可重复使用的先决条件，它为提高合成环境中生物催化剂的功能活力提供了可控策略。在此，我们使用分子动力学 (MD) 模拟，并探讨了 idase (MPO) 模型酶与经过验证的工业实施的选定金属有机框架（MOF；MIL-160 和 ZIF-8）之间的非共价相互作用。我们发现CA和MPO可以分别以201和501 kJ mol(-1)的最佳结合能与MIL-160结合，这受到酶和框架之间氢键发生率增加的强烈影响。另一方面，与疏水-疏水相互作用的发生相比，酶与 ZIF-8 结合的自由能受氢键网络的影响较小，疏水-疏水相互作用对 CA 产生 106 kJ mol(-1)，对 MPO 产生 201 kJ mol(-1)。
The catalytic efficiency and unrivaled selectivity with which enzymes convert substrates to products have been tapped for widespread chemical transformations within biomedical technology, biofuel production, gas sensing, and the upgrading of commodity chemicals, just to name a few. However, the feasibility of enzymes implementation is challenged by the lack of reusability and loss of native catalytic activity due to the irreversible biocatalyst denaturation at high temperatures and in the presence of industrial solvents. Enzyme immobilization, a prerequisite for enzyme reusability, offers controllable strategies for increased functional viability of the biocatalyst in a synthetic environment. Herein we used molecular dynamics (MD) simulations and probed the noncovalent interactions between model enzymes of idase (MPO), with selected metal-organic frameworks (MOFs; MIL-160 and ZIF-8) of proven industrial implementation. We found that the CA and MPO can bind to MIL-160 at optimal binding energies of 201 and 501 kJ mol(-1), respectively, that are strongly influenced by the increased incidence of hydrogen bonding between enzymes and the frameworks. The free energy of binding of enzymes to ZIF-8, on the other hand, was found to be less strongly influenced by hydrogen bonding networks relative to the occurrence of hydrophobic-hydrophobic interactions that yielded 106 kJ mol(-1) for CA and 201 kJ mol(-1) for MPO.