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- W2032124645 abstract "Penicillium canescens is a filamentous fungus that normally does not secrete notable levels of cellulase activity. Cellobiohydrolase I of P. canescens (PcCel7A) was homologously cloned into a host strain RN3-11-7 (niaD-) and then expressed under the control of a strong xylA promoter. Using three steps of chromatography, PcCel7A was purified. The enzyme displayed maximum activity at pH 4.0–4.5. PcCel7A was stable at 50 °C and pH 4.5 at least for 3 h, while at 60 °C it lost 45% of activity after 30 min of incubation. When equalized by protein concentration, PcCel7A demonstrated a higher performance in prolonged hydrolysis of Avicel and milled aspen wood than CBH I (Cel7A) from Trichoderma reesei, the most industrially utilized cellulase at this moment. The high catalytic efficiency of the PcCel7A makes it a potential candidate for industrial applications." @default.
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- W2032124645 date "2014-11-01" @default.
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- W2032124645 title "Homologous cloning, purification and characterization of highly active cellobiohydrolase I (Cel7A) from Penicillium canescens" @default.
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- W2032124645 doi "https://doi.org/10.1016/j.pep.2014.08.011" @default.
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