Zeolitic imidazolate framework (ZIF) has recently emerged as a promising material for the encapsulation of enzymes because of their high surface area and facile construction conditions. However, the enzymes are partial even completely inactive after encapsulation owing to the confinement effect and competing coordination, and otherwise, the alkaline environment caused by the protonation effect of 2-methylimidazole also damages enzyme molecules. Herein, a novel glutathione (GSH)-boosted one pot embedding strategy that enabled to rapidly encapsulate enzyme within GSH hybrid MOF (named enzyme@GMOF) with a high embedding efficiency was constructed. Hybrid of GSH and imidazole as synchronous ligands for GMOF to immobilize enzyme can offer sufficient well microenvironment for enzyme exhibiting high activity. The obtained catalysts (CAT@GZIF-67) displayed 9.0-fold higher catalytic activity than traditional ZIF-67 immobilized CAT (CAT@ZIF-67) and superior reusability and storage stability compared with CAT@ZIF-67 and free CAT. As one kind of biomacromolecules, bio-affinity of GSH can create an affinitive microenvironment for enzymes and reduce the influence of other factors during the use of biomacromolecules on their conformation and activity.

沸石咪唑酯骨架 (ZIF) 最近已成为一种很有前途的酶封装材料，因为它们具有高表面积和简便的构建条件。然而，由于限制效应和竞争配位，酶被包封后部分甚至完全失活，此外，2-甲基咪唑的质子化作用造成的碱性环境也会破坏酶分子。在此，构建了一种新型谷胱甘肽 (GSH) 增强的单罐包埋策略，能够以高包埋效率将酶快速包封在 GSH 杂化 MOF 中（命名为 enzyme@GMOF）。GSH和咪唑杂化物作为GMOF的同步配体固定化酶可以为酶的高活性提供充分良好的微环境。所得催化剂（CAT@GZIF-67）的催化活性比传统的 ZIF-67 固定化 CAT（CAT@ZIF-67）高 9.0 倍，与 CAT@ZIF-67 和游离 CAT 相比，其可重复使用性和储存稳定性更高。GSH作为生物大分子的一种，其生物亲和性可以为酶创造一个亲和的微环境，减少生物大分子在使用过程中其他因素对其构象和活性的影响。