Laccases　are　a　class　of　multi-copper　oxidases　with　industrial　potential.　In　this　study,　eight　laccases　(Lac1-8)　from　Cerrena　sp.　strain　HYB07,　a　white-rot　fungus　with　high　laccase　yields,　were　analyzed.　The　laccases　showed　moderate　identities　to　each　other　as　well　as　with　other　fungal　laccases　and　were　predicted　to　have　high　redox　potentials　except　for　Lac6.　Selected　laccase　isozymes　were　heterologously　expressed　in　the　yeast　Pichia　pastoris,　and　different　enzymatic　properties　were　observed.　Transcription　of　the　eight　laccase　genes　was　differentially　regulated　during　submerged　and　solid　state　fermentation,　as　shown　by　quantitative　real-time　polymerase　chain　reaction　and　validated　reference　genes.　During　6-day　submerged　fermentation,　Lac7　and　2　were　successively　the　predominantly　expressed　laccase　gene,　accounting　for　over　95%　of　all　laccase　transcripts.　Interestingly,　accompanying　Lac7　downregulation,　Lac2　transcription　was　drastically　upregulated　on　days　3　and　5　to　9958-fold　of　the　level　on　day　1.　Consistent　with　high　mRNA　abundance,　Lac2　and　7,　but　not　other　laccases,　were　identified　in　the　fermentation　broth　by　LC-MS/MS.　In　solid　state　fermentation,　less　dramatic　differences　in　transcript　abundance　were　observed,　and　Lac3,　7　and　8　were　more　highly　expressed　than　other　laccase　genes.　Elucidating　the　properties　and　expression　profiles　of　the　laccase　gene　family　will　facilitate　understanding,　production　and　commercialization　of　the　fungal　strain　and　its　laccases.