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Prof. Ahmed Abdel-Khalek Salem Salem Nayl :: Publications:

Title:
Lignocellulose degrading enzymes of Pleurotus sapidus
Authors: Not Available
Year: 2014
Keywords: Keywords: Lignocellulose biodegradation, P. sapidus, cellulase, xylanase, veratryl alcohol oxidase (VAO) and laccase.
Journal: Middle East Journal of Agriculture Research
Volume: 3
Issue: (4):
Pages: 1205-1213
Publisher: Not Available
Local/International: International
Paper Link: Not Available
Full paper Ahmed Abdel-Khalek Salem Nayl_Lignocellulose Degrading Enzymes of Pleurotus sapidus.pdf
Supplementary materials Not Available
Abstract:

The present study was performed for the production of some lignocellulose degrading enzymes from Pleurotus sapidus during the submerged cultivation. Moreover, characterization of lignocellulose degrading enzymes were evaluated. Basal medium containing 1% rice straw was the best for maximum lignocellulose degrading enzymes secretion by P. sapidus. Corn stalks were the most suitable carbon source for the production of cellulase, xylanase and laccase. While, saw dust gave low enzymes productivity. Maximum activity of cellulase, xylanase, veratryl alcohol oxidase (VAO) and laccase was obtained at concentration of 20 g/L of corn stalks. The most suitable concentration of yeast extract for maximum production of cellulase was 2 g/L. Moreover, maximum activity of xylanase, veratryl alcohol oxidase (VAO) and laccase was obtained at 2.5 g/ L of yeast extract. Maximum activity of cellulase and xylanase was obtained after 6 days of cultivation. On the other hand, veratryl alcohol oxidase (VAO) and laccase enzymes reached the maximum activity after 9 and 3 days of cultivation, respectively. The optimum temperature for cellulase and laccase activity was 50°C. While, xylanase and VAO enzymes reached the maximum activity at 60°C and 55°C, respectively. Concerning the optimum pH, cellulase and xylanase enzymes showed maximum activity at pH 3.5 and pH 4.0, respectively. However, pH 5.5 and pH 3.0 were optimum for the activity of VAO and laccase, respectively.

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