RESUMEN
Screening of the ligninolytic activity of basidiomycetes from the Culture Collection of the Komarov Botanical Institute, Russian Academy of Sciences, belonging to diterent taxonomic and ecological groups was performed. The patterns of the position of taxa of active producers of ligninolytic enzymes in the modern system of fungi were identified. Cluster analysis showed that the group of fungi with the greatest lign- inolytic and degradation potential includes representatives of the families Pleurotaceae, Polyporaceae, and Phanerochaetaceae, which perform the first stages of wood decomposition. As a result, species of interest for the further study of their oxidative potential and use in biotechnology were selected.
Asunto(s)
Basidiomycota , Lignina/metabolismo , Filogenia , Madera/microbiología , Basidiomycota/clasificación , Basidiomycota/enzimología , Basidiomycota/genéticaRESUMEN
Two promising strains of laccase producers--Lentinus strigosus 1566 and Steccherinum ochraceum 1833--were found by screening of basidiomycetes. The cultivation conditions increasing the enzyme yield were selected. The maximal laccase activity was observed in the case of submerged cultivation of the mycelium immobilized on polycaproamide fibers in rich media in the presence of 2 mM CuSO4 in combination with the optimal inducer, namely, 2,6-dimethylphenol for L. strigosus and 2,4-dimethylphenol for S. ochraceum. Under these conditions, the activity of S. ochraceum laccase amounted to 33.1 U/ml and that of L. strigosus, to 186.5 U/ml. Anthracene was transformed with S. ochraceum laccase, and its oxidation to anthraquinone was demonstrated by mass spectrometry.
Asunto(s)
Basidiomycota/enzimología , Lacasa/metabolismo , Antracenos/metabolismo , Basidiomycota/clasificación , Basidiomycota/crecimiento & desarrollo , Caprolactama/análogos & derivados , Medios de Cultivo , Micología/métodos , Oxidación-Reducción , PolímerosRESUMEN
The degree of heterogeneity of the proteolytic complex from the fungus Flammulina velutipes was studied by gel chromatography and analytical isoelectrofocusing. The fibrinolytic, thrombolytic, caseinolytic, endo- and aminopeptidase activities of the enzyme complex were compared to those of Aspergillus terricola and Streptomyces griseus proteinases. The proteolytic complex under study consists of at least two proteinases with pI 6.1 and 7.1, which possess fibrinolytic, thrombolytic and endopeptidase activities and of two aminopeptidases with pI 5.5 and 6.05. All these activities are inhibited by metal-chelating reagents. A low caseinolytic activity of the complex suggests that it can successfully be employed as a therapeutic agent.