Sika　deer　(Ceruse　nippon)　superoxide　dismutase　(SOD)　is　helpful　for　human　health.　In　this　paper,　of　Cervus　nippon　superoxide　dismutase　(SOD)　was　recombinantly　expressed　in　Pichia　pastoris　strain　GS115　and　then　determined　enzymatic　properties.　The　recombinant　Cu/Zn　SOD　was　purified　through　ultrafiltration　and　weak　anion　exchange　chromatography　(DEAE),　gel　filtration　to　obtain　specific　activity　of　17　647.1　U/mg.　Research　on　the　enzymatic　properties　showed　that　the　optimum　reaction　pH　of　the　SOD　was　about　8.0　and　the　optimal　reaction　temperature　was　30　.　The　SOD　was　relatively　stable　at　pH　5-9　and　below　70　.　Simulation　study　of　human　internal　digestion　found　that　this　recombinant　SOD　was　well　tolerant　for　protease　under　neutral　conditions　but　susceptible　to　gastric　acid　solution　with　severe　loss　of　enzyme　activity　due　to　acid　effect.　This　indicated　that　stomach　acid　is　the　main　problem　for　oral　intake　of　the　SOD.　This　study　is　proposed　to　be　basis　for　utilization　of　recombinant　Cervus　nippon　SOD.　©　2018,　Editorial　Office　of　Journal　of　CIFST.　All　right　reserved.