Laccases　are　polyphenol　oxidases　with　widespread　applications　in　various　industries.　In　the　present　study,　the　laccase　from　Cerrena　sp.　HYB07　was　immobilized　with　four　methods,　namely　entrapment　in　alginate,　covalently　binding　to　chitosan　as　well　as　formation　of　cross-linked　enzyme　aggregates　(CLEAs)　and　magnetic　CLEAs　(M-CLEAs).　The　activity　recovery　rates　of　the　immobilized　laccases　ranged　from　29%　to　68%.　Immobilization　elevated　the　reaction　temperature　optimum　and　reduced　substrate　specificity,　but　not　necessarily　the　turnover　rate.　pH　stability　of　immobilized　laccases　was　improved　compared　with　that　of　the　free　laccase,　especially　at　acidic　pH　values.　Thermal　inactivation　of　all　laccases　followed　a　simple　first-order　exponential　decay　model,　and　immobilized　laccases　displayed　higher　thermostability,　as　manifested　by　lower　thermal　inactivation　rate　constants　and　longer　enzyme　half-life　time.　Operational　stability　of　the　immobilized　laccase　was　demonstrated　by　decolorization　of　the　triphenylmethane　dye　malachite　green　(MG)　at　60　degrees　C.　MG　decolorization　with　free　laccase　was　accompanied　by　a　shift　of　the　absorption　peak　and　accumulation　of　a　stable,　colored　intermediate　tetradesmethyl　MG,　probably　due　to　lower　thermostability　of　the　free　laccase　and　premature　termination　of　the　degradation　pathway.　In　contrast,　complete　decolorization　of　MG　was　achieved　with　laccase　CLEAs　at　60　degrees　C.