Framework for Optimizing Polymeric Supports for Immobilized Biocatalysts by Computational Analysis of Enzyme Surface Hydrophobicity
Framework for Optimizing Polymeric Supports for Immobilized Biocatalysts by Computational Analysis of Enzyme Surface Hydrophobicity
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通过酶表面疏水性的计算分析优化固定化生物催化剂的聚合物载体的框架
DOI：
10.1021/acscatal.3c00264
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发表时间：
2023
期刊：
影响因子：
12.9
通讯作者：
Kaar, Joel L.
中科院分区：
文献类型：
--
作者：
Sánchez-Morán, Héctor;Gonçalves, Luciana Rocha;Schwartz, Daniel K.;Kaar, Joel L.
固定化是提高酶的可用性和稳定性的一个强有力的策略，在各种技术，采用生物催化。然而，导致稳定或不稳定的相互作用仍然知之甚少，并且可以稳定一种酶的支持物可能使另一种酶不稳定。采用化学异质性和复杂的无规共聚物刷作为支持，我们证明了一个合理的方法来估计最佳稳定的酶固定化支持的化学组成的酶表面疏水性的计算分析。这种方法进行了测试，通过固定化的范围内的酶与不同的功能和疏水性的可调统计无规共聚物刷支持组成的聚（乙二醇）甲基丙烯酸酯（PEGMA）和磺基甜菜碱甲基丙烯酸酯（SBMA）。值得注意的是，我们观察到作为刷组成的函数的酶性能大大改善，在高达90 °C的温度下催化活性的保留增强。此外，我们观察到在最佳温度下的活性增加多达20倍，相对于在最佳温度下的酶的未固定化形式的活性。最重要的是，我们的结果表明，刷支持物的最佳组成与酶表面的总体疏水性（ΔGsolv，总/面积）相关，这是由计算分析确定的。这种相关性提供了一个框架，选择聚合物刷支持酶的结构和稳定酶使用复杂的合成材料的基础上。
Immobilization is a powerful strategy for improving enzyme usability and stability in various technologies that employ biocatalysis. However, the interactions leading to stabilization or destabilization remain poorly understood, and a support that may stabilize one enzyme may destabilize another. Employing chemically heterogeneous and complex random copolymer brushes as supports, we demonstrate a rational approach toward estimating the chemical composition of an optimally stabilizing enzyme immobilization support by computational analysis of enzyme surface hydrophobicity. This approach was tested by immobilizing a range of enzymes with diverse functions and hydrophobicity on tunable statistical random copolymer brush supports composed of poly(ethylene glycol) methacrylate (PEGMA) and sulfobetaine methacrylate (SBMA). Remarkably, we observed greatly improved enzyme performance as a function of brush composition with enhancements in the retention of catalytic activity at temperatures as high as 90 °C. Additionally, we observed an increase in activity at the optimal temperature by as much as 20-fold relative to the activity at the optimal temperature of the unimmobilized form of the enzyme. Most significantly, our results showed that the optimal composition of the brush support correlated with the overall hydrophobicity of the enzyme surface (ΔGsolv,total/area), which was determined from computational analysis. This correlation provides a framework for the choice of polymer brush supports based on enzyme structure and stabilizing enzymes using complex synthetic materials.
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了解优化固定化酶和无规共聚物刷之间界面的设计规则。
影响因子：
9.5
作者：
Héctor Sánchez;James S. Weltz;D. K. Schwartz;Joel L. Kaar
通讯作者：
Joel L. Kaar
影响因子：
5.4
作者：
Chaparro Sosa, Andres F.;Black, Kenneth J.;Schwartz, Daniel K.
通讯作者：
Schwartz, Daniel K.
DOI：
10.1021/acs.langmuir.1c00828
发表时间：
2021-06-01
期刊：
Langmuir : the ACS journal of surfaces and colloids
影响因子：
--
作者：
Fritz PA;Bera B;van den Berg J;Visser I;Kleijn JM;Boom RM;Schroën CGPH
通讯作者：
Schroën CGPH
影响因子：
5.5
作者：
Fromel, Michele;Pester, Christian W.
通讯作者：
Pester, Christian W.
影响因子：
17.1
作者：
James S. Weltz;D. K. Schwartz;Joel L. Kaar
通讯作者：
James S. Weltz;D. K. Schwartz;Joel L. Kaar