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International Journal of Medicinal Mushrooms
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ISSN Imprimir: 1521-9437
ISSN En Línea: 1940-4344

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International Journal of Medicinal Mushrooms

DOI: 10.1615/IntJMedMushrooms.2019032706
pages 1115-1122

Comparison of Mono- and Dikaryotic Medicinal Mushrooms Lignocellulolytic Enzyme Activity

Eva Kachlishvili
The Agricultural University of Georgia, University Campus at Digomi, Tbilisi, Georgia
Aza Kobakhidze
The Agricultural University of Georgia, University Campus at Digomi, Tbilisi, Georgia
Mariam Rusitashvili
Agricultural University of Georgia, Tbilisi, Georgia
Ana Tsokilauri
Agricultural University of Georgia, Tbilisi, Georgia
Vladimir I. Elisashvili
Animal Husbandry and Feed Production Institute of Agricultural University of Georgia, 240 David Agmashenebeli alley, 0159 Tbilisi, Georgia


Mono- and dikaryotic medicinal mushroom strains isolated from four wood-rotting basidiomycete fruiting bodies were comparatively evaluated for laccase, manganese peroxidase, cellulase, and xylanase activities in submerged cultivation in glucose or mandarin peel−containing media. Mandarin peels appeared to be the preferred growth substrate for laccase production by both mono- and dikaryotic Trametes multicolor 511 and T. versicolor 5 while glucose favored laccase activity secretion by Pleurotus ostreatus 2175. Lignocellulose-deconstructing enzyme profiles were highly variable between the studied monokaryotic and dikaryotic strains. A distinctive superiority of enzyme activity of the dikaryotic Trametes versicolor 5 and P. ostreatus 2175 over the same species monokaryotic isolates was revealed. By contrast, laccase, cellulase, and xylanase activities of the monokaryotic strain of T. multicolor 511 were rather higher than those in the dikaryotic culture. At the same time, hydrolases activity of Schizophyllum commune 632 was practically independent of the origin of the fungal culture. The results suggest that the monokaryotic isolates derived from the basidiomycetes fruiting bodies inherit parental properties but the capacity of individual monokaryotic cultures to produce lignocellulose-deconstructing enzymes can vary considerably.


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