Abstract

Holocellulolytic accessory enzymes are very important in assisting hydrolysis of biomass. The use of these enzymes in the enzymatic hydrolysis of plant biomass is very important for obtaining building blocks in the concept of biorefinery. In previous studies, the mutant strain Trichoderma atroviride 102C1 was tested for production of endoglucanases, FPases and endoxylanases. This study aimed at evaluating the efficiency in holocellulolytic accessories enzymes production (b-glucosidase, b-xylosidase and a-L-arabinofuranosidase) by Trichoderma atroviride 102C1 using different lignocelluloses biomass as substrates. Accessory enzymes production was carried out in Erlenmeyer flasks containing Mandels salt medium, supplemented with different concentrations of sugarcane bagasse (SCB) and corn steep liquor (CSL), according to a Central Composite Rotational Design (CCRD). The fermentation system was incubated under agitation for 2 days / 28°C. For pH and temperature profile studies, a new CCRD was carried out. The best condition common to all enzymes, 55.4 U.mL-1 (β-glucosidase), 10.8 U.mL-1 (β-xylosidase) and 143.23 U.mL-1 (α-L-arabinofuranosidase), was observed when 2.5% (w/v) sugarcane bagasse (SCB) and 1.26% (w/v) of corn steep liquor (CSL) were used. All enzymes presented acidophilic characteristic in two different temperatures (44 and 55°C). The optimal profile characteristic for β-glucosidase and β-xylosidase activities were pH 5.0 and 3.0, respectively, both at 55°C, while for α-L-arabinofuranosidase it was pH 3.6 at 44°C. This study demonstrated the potential of T. atroviride 102C1 to produce three important holocellulolytic accessory enzymes in the presence of SCB and CSL, suggesting its use for enzymatic hydrolysis of lignocellulosic biomass.   Key words: Trichoderma atroviride 102C1, holocellulolytic enzymes, sugarcane bagasse, corn steep liquor.

Highlights

  • Plant cell walls are a source of renewable carbon present in nature as cellulose, hemicelluloses and lignin

  • The objective of the present study was to investigate the production of some hollocellulolytic accessory enzymes of T. atroviride 102C1, including β-glucosidase, β-xylosidase and α-Larabinofuranosidase, using submerged fermentation and, as main substrates, sugarcane bagasse in natura and corn steep liquor

  • Enzyme production was performed in submerged fermentation in Erlenmeyer flasks (125 ml) containing 25 ml of a modified culture medium (Mandels and Weber, 1969), in g.L-1: urea, 0.3; (NH4)2SO4, 1.4; KH2PO4, 2.0; CaCl2, 0.3; MgSO4.7H2O, 0.3; FeSO4.7H2O, 0.005; CoCl2.6H2O, 0.02; MnSO4.4H2O, 0.016; and ZnSO4.7H2O, 0.014 supplemented with sugarcane bagasse in natura (SCB) and corn steep liquor (CSL) at different concentrations, according to experimental design 22 central composite rotational design (CCRD)

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Summary

Introduction

Plant cell walls are a source of renewable carbon present in nature as cellulose, hemicelluloses and lignin. Worldwide attention has focused on the major biotechnological uses of the carbohydrates in agroindustrial by-products, as biomass syrups that have sugars with five or six carbons (derived from xylan and glucan). They can be used as carbon sources in industrial fermentations producing antibiotics, industrial enzymes, and bulk chemicals, including ethanol. For these purposes, the polysaccharides in the biomass must first be hydrolyzed (Gottschalk et al, 2010; Shinozaki et al, 2015)

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