White-rot　fungus　Cerrena　sp.　strain　HYB07　produces　laccase　with　high　yields　and　strong　decolorization　ability.　Cerrena　laccase　was　immobilized　by　preparing　Cross-linked　enzyme　aggregates　(CLEAs),　and　ammonium　sulfate　and　glutaraldehyde　were　the　optimal　precipitant　and　cross-linking　agent,　respectively.　An　activity　recovery　rate　of　68.1%　was　obtained　at　pH　8　after　precipitation　with　(NH4)(2)SO4　and　cross　linking　with　30　mM　glutaraldehyde　for　311　at　25　degrees　C.　Immobilized　Cerrena　laccase　demonstrated　improved　tolerance　to　NaCl,　metal　ions　and　organic　solvents.　NaCl　was　a　mixed-type　inhibitor　of　both　free　and　immobilized　laccases　with　2,　2＇-azino-bis　(3-ethylbenzothiazoline-6-sulfonic　acid)　as　the　substrate,　and　the　improvement　of　NaCl　resistance　by　laccase　immobilization　was　quantified　kinetically.　Laccase　CLEAs　had　higher　inhibition　constants　K-I　and　K-IS　compared　to　free　laccase,　suggesting　that　the　affinity　of　NaCl　to　laccase　was　attenuated　by　immobilization.　Laccase　CLEAs　also　displayed　greater　velocity　and　efficiency　in　Remazol　Brilliant　Blue　Reactive　decolorization　in　the　presence　of　NaCl　than　free　laccase.　Greater　differences　in　the　half　time　(t(1/2))　of　Remazol　Brilliant　Blue　Reactive　decolorization　by　free　and　immobilized　laccases　were　observed　with　increasing　NaCl　concentrations.　(C)　2016　Taiwan　Institute　of　Chemical　Engineers.　Published　by　Elsevier　B.V.　All　rights　reserved.