Enzyme　immobilization　is　critical　to　boosting　its　application　in　various　areas.　Covalent　organic　frameworks　(COFs)　are　ideal　hosts　for　enzyme　immobilization　due　to　their　porous　and　predesignable　structures.　Nevertheless,　the　construction　of　COFs-based　enzyme　immobilization　systems　with　high　activity　via　existing　immobiliza-tion　methods　(including　covalent　linkages　and　channel　entrapment)　remains　a　considerable　challenge.　Herein,　a　versatile　approach　was　introduced　to　encapsulate　enzymes　within　hollow　COF　capsule　(named　enzyme@COF)　using　metal-organic　frameworks　(including　ZPF-1(C8H11N4O4.5Zn),　ZIF-8(C8H10N4Zn),　and　ZIF-90-(C8H6N4O2Zn))　as　sacrificial　templates.　The　obtained　porous　COF　capsule　could　not　only　facilitate　the　efficient　mass　transfer　of　enzymatic　reactions　but　also　protect　enzymes　against　the　incompatible　conditions,　resulting　in　enhanced　activity　and　stability　of　the　encapsulated　enzymes.　Moreover,　this　approach　offered　an　opportunity　to　spatially　organize　multienzymes　in　COF　capsule　to　construct　enzyme　cascade　system.　For　instance,　glucose　oxidase　(GOx)　and　cytochrome　c　(Cyt　c)　were　coencapsulated　within　COF　capsule　to　construct　GOx-Cyt　c　cascade.　The　integration　of　GOx　and　Cyt　c　within　COF　capsule　achieved　similar　to　1.6-fold　improvement　in　catalytic　activity　than　that　of　free　enzymes　and　the　resultant　GOx-Cyt　c@COF　was　successfully　adopted　as　a　nanoreactor　for　the　sensitive　determination　of　glucose　in　serum.　This　work　provided　a　new　insight　into　the　design　of　COFs-based　enzyme　immobilization　systems.