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  • Selection of Trichoderma strains capable of increasing laccase production by Pleurotus ostreatus and Agaricus bisporus in dual cultures.

Selection of Trichoderma strains capable of increasing laccase production by Pleurotus ostreatus and Agaricus bisporus in dual cultures.

Journal of applied microbiology (2009-01-06)
C Flores, C Vidal, M R Trejo-Hernández, E Galindo, L Serrano-Carreón
초록

To select Trichoderma strains for enhanced laccase production in Pleurotus ostreatus or Agaricus bisporus cultures. Laccase production by P. ostreatus and A. bisporus was evaluated in liquid (axenic) and solid (dual cultures) malt extract medium. Oxidation of ABTS, DMP and syringaldazine was evaluated in order to assess the potential of Trichoderma strains to enhance laccase production by basidiomycetes. Selected Pleurotus-Trichoderma interactions yielded higher increases in laccase volumetric activity and an additional laccase isoform was produced. By contrast, Agaricus-Trichoderma interactions lead to smaller increases on laccase volumetric activity, probably as result of repression (or degradation) towards one of the laccases isoforms. The strains of P. ostreatus and A. bisporus assessed in this work showed good potential as laccase producers. The Trichoderma-mediated biological stimulation of laccase production by P. ostreatus and A. bisporus is relevant in order to develop highly productive processes. Extracellular laccases from basidiomycetes are produced only in small amounts. It is therefore important to increase process productivity for potential industrial applications. The results from this study enable the selection Trichoderma strains capable of increasing laccase production by P. ostreatus or A. bisporus in dual cultures.

MATERIALS
제품 번호
브랜드
제품 설명

Supelco
2,6-Dimethoxyphenol, analytical standard
Sigma-Aldrich
2,6-Dimethoxyphenol, natural, ≥96%
Sigma-Aldrich
2,6-Dimethoxyphenol, ≥98%, FG
Sigma-Aldrich
Syringaldazine, 98%
Sigma-Aldrich
2,6-Dimethoxyphenol, 99%
Sigma-Aldrich
Syringaldazine, indicator for laccase and peroxidase activity