Methodologies to enhance the activity and longevity of enzymes have occupied the significant positions in the enzyme-based biotechnologies. Enzyme immobilization in the solid support has been the most popular methods to fulfil the two key requirements. However, a few reports employed bicontinuous porous structures in nanoscale for mass transport and nanoscale space for efficient enzymatic functions simultaneously. Recently, we reported caging lipase in nanoporous covalent frameworks prepared from the polymer/poly-urea network mixtures via organic sol-gel(OSG) method. A new type of polymeric membrane with bicontinuous nanoporous morphology could be obtained through phase separation of polyethylene glycol(PEG) and poly-urea sol nanoparticles during solvent evaporation, followed by selective PEG extraction. The nanoporous membrane was employed as a trap for enzyme immobilization, with improved lifespan compared to free enzymes. To broaden the scope of the enzymes and examine the effects of confinement on the activity, we studied the enzymatic reactions from other categories of enzyme. The enzyme was immobilized in the nanopores by permeation through the nanoporous membrane applying an appropriate pressure. Enzymatic activity assay was performed using the enzyme-loaded membranes to investigate the optimized conditions in batch mode. The result shows the general applicability of caging in the nanoporous framework to promote the enzymatic activity in addition to a prolonged lifespan.