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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.    Electronic supplementary material  The online version of this article (doi:10.1186/s40643-017-0154-8) contains supplementary material, which is available to authorized users.

Green synthesis of enzyme/metal-organic framework composites with high stability in protein denaturing solvents