Abstract

Abstract In this study the solid-state fermentation for production of cellulolytic enzymes by the fungus Gelatoporia subvermispora was optimized. The enzyme activities on filter paper, exo-cellulase, endo-cellulase and xylanase were determined. A Plackett-Burman design (PB) was used to determine the most significant variables (moisture content of substrate, inoculum density, corn steep liquor concentration, pH and peptone concentration) in the enzyme production for each substrate (sugarcane bagasse, sewage sludge and rice straw). The highest value for filter paper activity was obtained using sugarcane bagasse as substrate. The sewage sludge was an excellent medium for the production of xylanase and exo-cellulases. The endo-cellulase activity was similar in all substrates tested. This is the first report of the Gelatoporia genus for the production of cellulolytic enzymes, being a promising strain for this purpose.

Highlights

  • The new concept of ethanol production corresponds to utilizing lignocellulosic biomass such as low-cost agricultural, forest residues and wood process wastes (Sims et al, 2008)

  • Sewage sludge was an excellent medium for production of extracts with high exo-cellulase and xylanase activities

  • The production of cellulolytic enzymes with endo-cellulase activities was similar in all substrates tested

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Summary

Introduction

The new concept of ethanol (or bioethanol) production corresponds to utilizing lignocellulosic biomass such as low-cost agricultural, forest residues and wood process wastes (Sims et al, 2008). The conversion of lignocellulosic biomass into fuels can be achieved using enzyme systems acting in order to hydrolyze biomass to glucose. It is well established that hydrolytic efficiency is a result of the synergistic actions of multicomponent enzymatic systems, containing at least three major groups of enzymes: endo-glucanases (E.C. 3.2.1.4), which hydrolyze the cellulose polymer internally, exposing reducing and non-reducing ends; exo-glucanases or cellobiohydrolases (E.C. 3.2.1.91), which act on the reducing and non-reducing ends, releasing cellobiose and cellooligosaccharides; and β–glucosidases (E.C. 3.2.1.21), which cleave cellobiose, liberating two molecules of glucose–the end product (Maeda et al, 2011; Delabona et al, 2013; Gottschalk et al, 2010).

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