Aflatoxin　B-1(AFB(1))　is　a　known　toxic　human　carcinogen　and　can　be　detoxified　by　laccases,　which　are　multicopper　oxidases　that　convert　several　environmental　pollutants　and　toxins.　In　this　study,　a　new　laccase　that　could　catalyze　AFB(1)degradation　was　purified　and　identified　from　the　white-rot　fungusCerrena　unicolor6884.　The　laccase　was　purified　using　(NH4)(2)SO(4)precipitation　and　anion　exchange　chromatography,　and　then　identified　as　Lac　2　through　zymogram　and　UHPLC-MS/MS　based　on　the　Illumina　transcriptome　analysis　ofC.　unicolor6884.　Six　putative　laccase　protein　sequences　were　obtained　via　functional　annotation.　Thelac　2cDNA　encoding　a　full-length　protein　of　512　amino　acids　was　cloned　and　sequenced　to　expand　the　fungus　laccase　gene　library　for　AFB(1)detoxification.　AFB(1)degradation　by　Lac　2　was　conducted　in　vitro　at　pH　7.0　and　45　degrees　C　for　24　h.　The　half-life　of　AFB(1)degradation　catalyzed　by　Lac　2　was　5.16　h.　Acetosyringone　(AS),　Syrinagaldehyde　(SA)　and　[2,2　＇　-azino-bis-(3-ethylbenzothiazoline-6-sulfonic　acid)]　(ABTS)　at　1　mM　concentration　seemed　to　be　similar　mediators　for　strongly　enhancing　AFB(1)degradation　by　Lac　2.　The　product　of　AFB(1)degradation　catalyzed　by　Lac　2　was　traced　and　identified　to　be　Aflatoxin　Q(1)(AFQ(1))　based　on　mass　spectrometry　data.　These　findings　are　promising　for　a　possible　application　of　Lac　2　as　a　new　aflatoxin　oxidase　in　degrading　AFB(1)present　in　food　and　feeds.