Controllable Synthesis of Hollow Microtubular Covalent Organic Frameworks as an Enzyme-Immobilized Platform for Enhancing Catalytic Activity.

Controllable Synthesis of Hollow Microtubular Covalent Organic Frameworks as an Enzyme-Immobilized Platform for Enhancing Catalytic Activity.
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DOI:
10.1021/acsami.1c16386
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发表时间:
2021-11
影响因子:
9.5
通讯作者:
Chao Zhong;Wende Ma;Yanting He;Dan Ouyang;Guorong Li;Yixin Yang;Qiong Zheng;Huan Huang;Zongwei Cai;Zian Lin
Chao Zhong;Wende Ma;Yanting He;Dan Ouyang;Guorong Li;Yixin Yang;Qiong Zheng;Huan Huang;Zongwei Cai;Zian Lin
中科院分区:
材料科学2区
文献类型:
--
作者:
Chao Zhong;Wende Ma;Yanting He;Dan Ouyang;Guorong Li;Yixin Yang;Qiong Zheng;Huan Huang;Zongwei Cai;Zian Lin

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尽管在共价有机框架(COFs)的合成方面取得了巨大的成就,但精确构建具有良好纳米/微米结构的COFs提出了严峻的挑战。在此,我们介绍了一种简单的无模板可控合成中空微管COFs的策略。当精心调节催化酸的浓度时,所得COF表现出从微纤维到中空微管结构的自发形态转变。此外,所制备的COF表现出高结晶度,良好定义的中空管状形态,和高表面积(约2600 m2/g)。中空微管状COFs具有独特的形态结构,是一种理想的酶载体材料。所得的生物复合材料显示出高催化性能,并可成功地应用于快速和高效的蛋白质水解。该研究为无模板法可控合成中空微管状COFs开辟了一条新的途径,拓展了COFs作为酶固定化平台的应用前景。
Despite great achievement that has been made in the synthesis of covalent organic frameworks (COFs), precise construction of COFs with well-defined nano/microstructures poses a rigorous challenge. Herein, we introduce a simple template-free strategy for controllable synthesis of hollow microtubular COFs. The obtained COFs show a spontaneous morphology transformation from a microfiber to a hollow microtubular structure when the concentrations of catalytic acid are regulated elaborately. Furthermore, the as-prepared COFs exhibit high crystallinity, well-defined hollow tubular morphology, and high surface areas (∼2600 m2/g). Taking the advantages of the unique morphological structure, the hollow microtubular COFs can serve as an ideal host material for enzymes. The resultant biocomposites show high catalytic performance and can be successfully applied to rapid and high-efficiency proteolysis of proteins. This work blazes a trail for controllable synthesis of the hollow microtubular COFs through a template-free process and expands the application of COFs as a promising platform for enzyme immobilization.