Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/354196
Type: Artigo
Title: Determination of enzyme (cellulase from trichoderma reesei) kinetic parameters in the enzymatic hydrolysis of H2so4-catalyzed hydrothermally pretreated sugarcane bagasse at high-solids loading
Author: Tovar, Laura Plazas
Lopes, Emilia Savioli
Wolf Maciel, Maria Regina
Maciel Filho, Rubens
Abstract: Enzymatic kinetic studies of celulignin material obtained from acid-catalyzed hydrothermally pretreated sugarcane bagasse at high-solids loading (S/25%), acid concentration (A) equal to 1.0; 2.0 and 3.0% w/v and pretreatment time (t(P)) equal to 30; 90 and 150 min were carried out using the synergistic action of cellulase from T. reesei and cellobiase from Aspergillus niger. The kinetic experiments were carried out at 50 degrees C, 150 rpm and 3 h with substrate (water insoluble solids after pretreatment-WIS) loading range between 30 gsubstrate/L-sol and 100 gsubstrate/L-sol, and mixed with cellulase (at 5.0; 15.0; 30.0 and 60.0 FPU cellulase/(gsubstrate)) and beta-glucosidase (at 33.0 IU beta-glucosidase/gsubstrate) enzymes. A Michaelis-Menten dependence on the cellulase from T. reesei concentration and substrate concentration plots were obtained based on experimental data. The rate constant, K-m and maximum reaction rate attainable, V-max were determined to characterize the cellulase-catalyzed reaction. Results showed that the cellulase from T. reesei behavior was highly specific for each WIS fraction obtained under a combination of [A-S-t(P)] where V-max varies greatly as enzyme (cellulase) concentration rises. For example, V-max values when considered a substrate obtained at [1.0% w/v-25%-30 min] and [3.0% w/v 25% -30 min] using 5.0 FPU cellulase/(gsubstrate(WIS)) and [1.0% w/v-25%-90 min] and [3.0% w/v-25%-90 min] using 60.0 FPU cellulase/(gsubstrate(WIS)) were 5.96+/-0.27 gGLC/L(SOL)h; 2.90+/-0.05 gGLC/L(SOL)h; 5.16+/-0.18 gGLC/L(SOL)h; 7.48+/-0.81 gGLC/Lh, respectively. Dependence on the K-m of enzyme-catalyzed reaction exhibited a considerably variation with the substrate nature and the enzymatic kinetic conditions establishing that K-m for the cellulase from T. reesei-substrate complex was between 54.81 g(GLC)/L-SOL and 209.99 g(GLC/)L(SOL)
Subject: Biomassa
Cana-de-açúcar
Bioetanol
Country: Itália
Editor: Associazione Italiana di Ingegneria Chimica
Rights: Fechado
Identifier DOI: 10.3303/CET1543096
Address: https://www.cetjournal.it/index.php/cet/article/view/CET1543096
Date Issue: 2015
Appears in Collections:FEQ - Artigos e Outros Documentos

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