Capsules　with　designable　chemical　and　textural　structures　provide　a　universal　and　versatile　platform　for　enzyme　immobilization.　Herein,　a　capsular　biocatalyst　(TpBD　CP@Lactate　dehydrogenase@Silica　capsules,　TLS　capsules)　was　developed　by　entrapping　enzyme　within　the　wall　of　conjugated　polymer　(CP)/silica　hybrid　capsules.　The　porous　wall　of　TLS　capsules　provided　sufficient　adsorption　sites　for　a　high　enzyme　loading　capacity　of　102.79　mg　g−1,　as　well　as　abundant　and　shorter　substrate　transfer　pathways,　resulting　in　catalytic　efficiency　of　133.0　%　that　of　free　LDH.　TLS　capsules　achieved　an　optimal　balance　between　substrate　enrichment　and　diffusion　at　a　30　mmol　L−1　Na2SiO3　solution　concentration,　resulting　in　a　14　%　increase　in　catalytic　activity.　Furthermore,　the　mineralized　silica　layer　provided　suitable　enzyme-carrier　interactions,　ensuring　the　structural　stability　of　the　enzyme　under　extreme　conditions.　TLS　capsules　maintained　over　80.47　%　relative　activity　after　eight　cycles.　Our　work　broadens　the　scope　for　developing　and　applying　enzyme　immobilization　platforms.　©　2025　Elsevier　Ltd