A　method　of　laccase　immobilization　was　developed　by　ZrO2　synthesized　via　biomineralization,　which　was　prepared　by　encapsulating　laccase　in　the　zirconia　nanoparticles　with　the　lysozyme　as　the　inducer,　and　the　recovery　rate　of　enzyme　activity　was　59%.　Field　emission　scanning　electron　microscope　(FESEM),　energy　dispersive　spectrometer　(EDS),　and　thermal　gravimetric　analyzer　(TGA)　were　used　to　characterize　ZrO2　nanoparticles　before　and　after　the　enzyme　immobilization.　The　results　proved　that　laccase　was　immobilized　in　ZrO2　successfully　and　lysozyme　was　not　only　induced　the　formation　of　zirconia　but　also　acted　as　a　biological　template　encapsulated　by　ZrO2.　Enzymatic　properties　of　immobilized　laccase　by　biomimetic　synthesis　were　also　explored.　The　optimum　pH　and　temperature　of　immobilized　laccase　were　3　and　70,　respectively.　Compared　with　free　enzyme,　the　pH　and　temperature　stability　of　immobilized　laccase　were　significantly　increased.　The　activity　of　the　immobilized　laccase　was　95%　of　the　original　activity　after　storing　for　30　days　at　4,　and　the　activity　was　still　60%　of　the　initial　enzyme　activity　after　recycling　5　times.　Moreover,　the　immobilized　laccase　was　used　in　the　decolorization　of　malachite　green　and　the　experimental　result　showed　that　the　decolorization　rate　of　the　malachite　green　was　more　than　95%　within　6h.　Additionally　it　proved　that　the　immobilized　laccase　decolorized　malachite　green　by　both　of　adsorption　and　degradation　effects　through　the　UV-visible　spectroscopy　analysis.　©　2018,　Chemical　Industry　Press.　All　right　reserved.