Laccases　(EC　1.10.3.2)　are　a　class　of　multi-copper　oxidases　with　important　industrial　values.　A　basidiomycete　strain　Cerrena　sp.　HYB07　with　high　laccase　yield　was　identified.　After　cultivation　in　the　shaking　flask　for　4　days,　a　maximal　activity　of　210.8　U　mL(-1)　was　attained.　A　58.6-kDa　laccase　(LacA)　with　7.2%　carbohydrate　and　a　specific　activity　of　1952.4　U　mg(-1)　was　purified.　2,2＇-Azino-bis　(3-ethylbenzothiazoline-6-sulfonic　acid)　was　the　optimal　substrate,　with　K-m　and　k(cat)　being　93.4　mu　M　and　2468.0　s(-1),　respectively.　LacA　was　stable　at　60　degrees　C,　pH　5.0　and　above,　and　in　organic　solvents.　Metal　ions　Na+,　K+,　Ca2+,　Mg2+,　Mn2+,　Zn2+　enhanced　LacA　activity,　while　Fe2+　and　Li+　inhibited　LacA　activity.　LacA　decolorized　structurally　different　dyes　and　a　real　textile　effluent.　Its　gene　and　cDNA　sequences　were　obtained.　Putative　cis-acting　transcriptional　response　elements　were　identified　in　the　promoter　region.　The　high　production　yield　and　activity,　robustness　and　dye　decolorizing　capacity　make　LacA　and　Cerrena　sp.　HYB07　potentially　useful　for　industrial　and　environmental　applications　such　as　textile　finishing　and　wastewater　treatment.