Bioinspired Immobilization of Glycerol Dehydrogenase by Metal Ion-Chelated Polyethyleneimines as Artificial Polypeptides.
Bioinspired Immobilization of Glycerol Dehydrogenase by Metal Ion-Chelated Polyethyleneimines as Artificial Polypeptides.
复制标题
金属离子螯合聚乙烯亚胺人工多肽仿生固定甘油脱氢酶
DOI：
10.1038/srep24163
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发表时间：
2016-04-07
影响因子：
4.6
通讯作者：
Wang S
中科院分区：
文献类型：
--
作者：
Zhang Y;Ren H;Wang Y;Chen K;Fang B;Wang S
在这项研究中，一种新的，简单的和普遍适用的策略，多聚体氧化还原酶固定与多层次的相互作用，并涉及活性和稳定性的增强。线性聚乙烯亚胺（PEI）是具有跨越宽范围的分子量的柔性阳离子聚合物，并且是用于酶固定化的生物相容性框架的合适的仿生多肽。以金属离子螯合的线性聚乙烯亚胺为骨架，通过氢键、静电力和配位键等相互作用固定化甘油脱氢酶。制备了直径为250-650 nm的纳米颗粒，其表现出1.4倍的催化效率增强。重要的是，在85 °C下，固定化GDH在水相中的半衰期提高了5.6倍。基于固定化酶的形态和功能研究，提出了PEI-金属-GDH复合物中多级相互作用形成的机理说明。该方法具有成本低、操作简便、活性保留率高、稳定性好等优点，是一种具有广泛应用前景的多聚体酶固定化技术。
In this study, a novel, simple and generally applicable strategy for multimeric oxidoreductase immobilization with multi-levels interactions was developed and involved activity and stability enhancements. Linear polyethyleneimines (PEIs) are flexible cationic polymers with molecular weights that span a wide range and are suitable biomimic polypeptides for biocompatible frameworks for enzyme immobilization. Metal ion-chelated linear PEIs were applied as a heterofunctional framework for glycerol dehydrogenase (GDH) immobilization by hydrogen bonds, electrostatic forces and coordination bonds interactions. Nanoparticles with diameters from 250–650 nm were prepared that exhibited a 1.4-fold enhancement catalytic efficiency. Importantly, the half-life of the immobilized GDH was enhanced by 5.6-folds in aqueous phase at 85 °C. A mechanistic illustration of the formation of multi-level interactions in the PEI-metal-GDH complex was proposed based on morphological and functional studies of the immobilized enzyme. This generally applicable strategy offers a potential technique for multimeric enzyme immobilization with the advantages of low cost, easy operation, high activity reservation and high stability.