1.Bioconversion of lignocellulosic residues by Agrocybe cylindracea and Pleurotus ostreatus mushroom fungi--assessment of their effect on the final product and spent substrate properties.
Koutrotsios G1, Mountzouris KC2, Chatzipavlidis I1, Zervakis GI3. Food Chem. 2014 Oct 15;161:127-35. doi: 10.1016/j.foodchem.2014.03.121. Epub 2014 Apr 3.
Nine agro-industrial and forestry by-products were subjected to solid-state fermentation by Agrocybe cylindracea and Pleurotus ostreatus, and the process and end-products were comparatively evaluated. Grape marc waste plus cotton gin trash was the best performing medium for both fungi, while substrate composition had a marked effect on most cultivation parameters. Biological efficiency was positively correlated with nitrogen, lignin and ash, and negatively with hemicelluloses and carbohydrate content of substrates. Spent substrates demonstrated high reductions in hemicelluloses and cellulose in contrast to lignin; fibre fractions were correlated with nitrogen, fat and ash content of initial materials, while residual mycelial biomass was affected by mushroom productivity. Mushroom proximate analysis revealed significant variations of constituents depending on the substrate. Crude protein and fat were correlated with substrates nitrogen for both species.
2.Molecular characterization of the Pri3 gene encoding a cysteine-rich protein, specifically expressed during fruiting initiation within the Agrocybe aegerita complex.
Sirand-Pugnet P1, Labarère J. Curr Genet. 2002 Apr;41(1):31-42. Epub 2002 Mar 23.
Coding and regulating sequences of Pri3 (a novel gene specifically expressed in both nucleus types of dikaryons during fruiting initiation) were compared within nine strains of the Agrocybe aegerita complex originating from Europe, Asia and Latin America. Highly homologous coding sequences were found; and the 95-amino-acid-long PRI3 deduced proteins all shared eight cysteines and eight glycines, a putative signal peptide suggesting an extra-cellular localization, a protein kinase C site (T(70)) and a cAMP-dependent kinase site (S(74)). The PRI3 proteins presented no significant homologies with already known proteins and constitute a new class of small cysteine-rich proteins. Within the 5' uncoding regions, two leader introns and a putative upstream regulating sequence resembling the QA1-F activator site were highly conserved. Comparison of the gene sequences within the A. aegerita complex suggested a divergent evolution of the European and Asian/Latin American groups of genes.