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- W2107353436 abstract "The glycoside hydrolase family 15 (glucoamylases) comprises exohydrolases that catalyze the release of β-glucose units from the non-reducing ends of polymersaccharides. A glucoamylase gene (PnGlu1) from Pholiota nameko was cloned and characterized. The 1743 bp coding region of PnGlu1 encoded a 581-amino acid polypeptide with a signal peptide comprising 17 amino acids at the N-terminal end. In addition to showing high homology with the glucoamylase from Laccaria bicolor, the PnGlu1 gene encodes a protein with an N-terminal catalytic domain and a C-terminal starch-binding domain. Quantitative reverse transcription-PCR (qRT-PCR) was used to examine the role of the glucoamylase gene in the growth of mycelia when the fungus was cultured in minimal medium containing glucose or soluble starch, as well as the growth of mycelia and tissue development in fruit bodies at different stages. The findings suggested that expression of PnGlu1 in the dikaryon strain was higher than observed in the monokaryon strain, with PnGlu1 expression induced by soluble starch. However, during cultivation on sawdust medium, the expression of PnGlu1 decreased drastically in dikaryotic mycelia after mycelial stimulation (kinkaki). Conversely, although PnGlu1 expression was not observed during fruit body development, the glucoamylase enzyme activity was stable and the glucose content increased dramatically. These results suggested that at least two glucoamylases are produced by P. nameko; the one cloned in this study, which only catalyzed the conversion of soluble starch into glucose and which, in turn, increased mycelial growth, and another glucoamylase that may be involved in fruit body formation." @default.
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- W2107353436 date "2011-01-01" @default.
- W2107353436 modified "2023-09-26" @default.
- W2107353436 title "Expression of genes for the glucoamylases (glycoside hydrolase family 15, GH15) in edible mushrooms." @default.
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