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固定化酶:在分子水平上理解酶与表面的相互作用

Immobilized enzymes: understanding enzyme - surface interactions at the molecular level.

作者信息

Hoarau Marie, Badieyan Somayesadat, Marsh E Neil G

机构信息

Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.

出版信息

Org Biomol Chem. 2017 Nov 22;15(45):9539-9551. doi: 10.1039/c7ob01880k.

Abstract

Enzymes immobilized on solid supports have important and industrial and medical applications. However, their uses are limited by the significant reductions in activity and stability that often accompany the immobilization process. Here we review recent advances in our understanding of the molecular level interactions between proteins and supporting surfaces that contribute to changes in stability and activity. This understanding has been facilitated by the application of various surface-sensitive spectroscopic techniques that allow the structure and orientation of enzymes at the solid/liquid interface to be probed, often with monolayer sensitivity. An appreciation of the molecular interactions between enzyme and surface support has allowed the surface chemistry and method of enzyme attachement to be fine-tuned such that activity and stability can be greatly enhanced. These advances suggest that a much wider variety of enzymes may eventually be amenable to immobilization as green catalysts.

摘要

固定在固体载体上的酶在工业和医学领域有着重要应用。然而,其应用受到固定化过程中常常伴随的活性和稳定性显著降低的限制。在此,我们综述了近期在理解蛋白质与支撑表面之间分子水平相互作用方面取得的进展,这些相互作用导致了稳定性和活性的变化。各种表面敏感光谱技术的应用推动了这一理解,这些技术能够以单层灵敏度探测酶在固液界面的结构和取向。对酶与表面载体之间分子相互作用的认识使得表面化学和酶固定方法得以精细调整,从而可大幅提高活性和稳定性。这些进展表明,最终可能会有更多种类的酶适合作为绿色催化剂进行固定化。

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