Fast　and　high-efficiency　protein　digestion　is　essential　for　high-throughput　proteome　analysis.　Herein,　a　new　kind　of　trypsin-inorganic　hybrid　nanocomposites　were　room-temperature　synthesized　based　on　self-assembly　stragety,　where　trypsin　and　nickel　phosphate　(Ni-3(PO4)(2))　was　used　as　organic　and　inorganic　ligands,　respectively.　The　general　applicability　of　the　synthetic　method　was　also　confirmed　by　using　a　series　of　other　metal　phosphates　including　Mg2+,　Ba2+,　Zn2+,　and　Co2+.　The　as-prepared　trypsin-inorganic　hybrid　nanocomposites　with　flower-like　morphology　showed　higher　enzymatic　acticity　(206　%　enhancement)　and　faster　catalytic　kinetics　than　the　free　trypsin.　Taking　the　merits　togethers　as　mentioned　above,　the　hybrid　nanocomposites　could　be　employed　as　an　immmobilized　enzyme　reactor　(IMER)　for　fast　and　high-efficiency　protein　digestion.　The　peptide　mass　fingerprint　analysis　of　the　model　proteins　demonstrated　that　the　coverage　rate　of　the　sequences　treated　by　IMER　could　bear　comparsion　with　that　of　the　free　one,　but　the　digestion　time　was　shorten　from　12　h　to　1　min.　In　addition,　the　IMER　showed　a　good　applicability　for　complex　human　serum　sample,　showing　a　promising　potential　in　proteomics　research.