Pretreated Sugarcane Bagasse
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2021 ◽  
Vol 46 (1SI) ◽  
pp. 53-67
J�ssica de Araujo Zanoni ◽  
Isabela Brunozi De Oliveira ◽  
Olavo Micali Perrone ◽  
Julieth Ordu�a Ortega ◽  
Maur�cio Boscolo ◽  

The xylanolytic enzyme complex hydrolyzes xylan, and these enzymes have various industrial applications. The goal of this work was to characterize the endoxylanases produced by the thermophilic fungus Rasamsonia emersonii in solid-state cultivation. Tests were carried out to evaluate the effects of pH, temperature, glycerol and phenolic compounds on enzyme activity. Thermal denaturation of one isolated enzyme was evaluated. The crude extract from R. emersonii was applied to breakdown pretreated sugarcane bagasse, by quantifying the release of xylose and glucose. The optimum pH value for the crude enzymatic extract was 5.5, and 80 �C was the optimum temperature. Regarding the stability of the crude extract, the highest values occurred between the pH ranges from 4 to 5.5. Several phenolic compounds were tested, showing an increase in enzymatic activity on the crude extract, except for tannic acid. Zymography displayed four corresponding endoxylanase bands, which were isolated by extraction from a polyacrylamide gel. The thermodynamic parameters of isolated Xylanase C were evaluated, showing a half-life greater than 6 h at 80 �C (optimum temperature), in addition to high melting temperature (93.3 �C) and structural resistance to thermal denaturation. Pretreated sugarcane bagasse breakdown by the crude enzymatic extract from R. emersonii has good hemicellulose conversion to xylose.

Catalysts ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 340
Wilson Morais Junior ◽  
Thályta Pacheco ◽  
Shipeng Gao ◽  
Pedro Martins ◽  
José Guisán ◽  

The saccharification of sugarcane bagasse by enzymatic hydrolysis is one of the most promising processes for obtaining fermentable sugar to be used in the production of second-generation ethanol. The objective of this work was to study the immobilization and stabilization of two commercial enzymes: Endocellulase (E-CELBA) in dextran coated iron oxide magnetic nanoparticles activated with aldehyde groups (DIOMNP) and β-glucosidase (E-BGOSPC) in glyoxyl agarose (GLA) so that their immobilized derivatives could be applied in the saccharification of pretreated sugarcane bagasse. This was the first time that the pretreated sugarcane bagasse was saccharified by cascade reaction using a endocellulase immobilized on dextran coated Fe2O3 with aldehyde groups combined with a β-glucosidase immobilized on glyoxyl agarose. Both enzymes were successfully immobilized (more than 60% after reduction with sodium borohydride) and presented higher thermal stability than free enzymes at 60, 70, and 80 °C. The enzymatic hydrolysis of the sugarcane bagasse was carried out with 15 U of each enzyme per gram of bagasse in a solid-liquid ratio of 1:20 for 48 h at 50 °C. Under these conditions, 39.06 ± 1.18% of the cellulose present in the pretreated bagasse was hydrolyzed, producing 14.11 ± 0.47 g/L of reducing sugars (94.54% glucose). In addition, DIOMNP endo-cellulase derivative maintained 61.40 ± 1.17% of its enzymatic activity after seven reuse cycles, and GLA β-glucosidase derivative maintained up to 58.20 ± 1.55% of its enzymatic activity after nine reuse cycles.

Julia Ponce ◽  
João Gabriel da Silva Andrade ◽  
Luciana Nunes dos Santos ◽  
Milena Keller Bulla ◽  
Beatriz Cervejeira Bolanho Barros ◽  

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