Objectives

Enzyme/metal-organic framework composites with high stability in protein denaturing solvents were reported in this study.

Results

Encapsulation of enzyme in metal-organic frameworks (MOFs) via co-precipitation process was realized, and the generality of the synthesis was validated by using cytochrome c, horseradish peroxidase, and Candida antarctica lipase B as model enzymes. The stability of encapsulated enzyme was greatly increased after immobilization on MOFs. Remarkably, when exposed to protein denaturing solvents including dimethyl sulfoxide, dimethyl formamide, methanol, and ethanol, the enzyme/MOF composites still preserved almost 100% of activity. In contrast, free enzymes retained no more than 20% of their original activities at the same condition. This study shows the extraordinary protecting effect of MOF shell on increasing enzyme stability at extremely harsh conditions.

Conclusion

The enzyme immobilized in MOF exhibited enhanced thermal stability and high tolerance towards protein denaturing organic solvents.

中文翻译：

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在蛋白质变性溶剂中具有高稳定性的酶/金属-有机骨架复合材料的绿色合成。

目标

这项研究报道了在蛋白质变性溶剂中具有高稳定性的酶/金属-有机骨架复合材料。

结果

通过共沉淀过程实现了酶在金属有机骨架（MOF）中的包封，并以细胞色素c，辣根过氧化物酶和南极假丝酵母脂肪酶B为模型酶验证了合成的一般性。固定在MOFs上后，封装酶的稳定性大大提高。值得注意的是，当暴露于蛋白质变性溶剂（包括二甲基亚砜，二甲基甲酰胺，甲醇和乙醇）时，酶/ MOF复合材料仍保留了几乎100％的活性。相反，在相同条件下，游离酶保留的活性不超过其原始活性的20％。这项研究表明，在极度苛刻的条件下，MOF壳对提高酶稳定性具有非凡的保护作用。

结论

固定在MOF中的酶表现出增强的热稳定性和对蛋白质变性有机溶剂的高耐受性。