World J. Microbiol. Biotechnol.

Mycelia Sterilia YY-5, an endophytic fungus isolated from Rhus Chinensis Mill, was used in SSF for laccase production using steam-exploded wheat straw (SEWS). The fermentation period of YY-5 in solid state fermentation (SSF) shortened to 4 days compared with 5 days of submerged liquid fermentation (SmF) and the maximum laccase activity was 678.1 IU g(-1) substrate. The steam-explosion intensity (Log(10)R(0)) of SEWS had a significant effect on the growth of YY-5 and laccase activity, since SEWS could provide enough carbon source for YY-5 and inducers for laccase. The optimum SSF conditions using SEWS with Log(10)R(0) = 3.597 as substrate were: inoculating with liquid inocula, keeping the solid-to-liquid ratio (S/L) for 1:4 and cultivating at 26 degrees C. Under the optimum fermentation condition the laccase activity of YY-5 reached 849.5 +/- 42.5 IU g(-1) substrate. The enzyme composition analysis indicated that laccase was the dominant enzyme of YY-5. Assayed with SDS-PAGE and active PAGE electrophoresis, the molecular weight of YY-5 laccase was approximately 45 kDa.Mycelia Sterilia YY-5, an endophytic fungus isolated from Rhus Chinensis Mill, was used in SSF for laccase production using steam-exploded wheat straw (SEWS). The fermentation period of YY-5 in solid state fermentation (SSF) shortened to 4 days compared with 5 days of submerged liquid fermentation (SmF) and the maximum laccase activity was 678.1 IU g(-1) substrate. The steam-explosion intensity (Log(10)R(0)) of SEWS had a significant effect on the growth of YY-5 and laccase activity, since SEWS could provide enough carbon source for YY-5 and inducers for laccase. The optimum SSF conditions using SEWS with Log(10)R(0) = 3.597 as substrate were: inoculating with liquid inocula, keeping the solid-to-liquid ratio (S/L) for 1:4 and cultivating at 26 degrees C. Under the optimum fermentation condition the laccase activity of YY-5 reached 849.5 +/- 42.5 IU g(-1) substrate. The enzyme composition analysis indicated that laccase was the dominant enzyme of YY-5. Assayed with SDS-PAGE and active PAGE electrophoresis, the molecular weight of YY-5 laccase was approximately 45 kDa