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Electronic Journal of Biotechnology
Universidad Católica de Valparaíso
ISSN: 0717-3458
Vol. 18, No. 4, 2015, pp. 314-319
Bioline Code: ej15051
Full paper language: English
Document type: Research Article
Document available free of charge

Electronic Journal of Biotechnology, Vol. 18, No. 4, 2015, pp. 314-319

 en Production of β-glucosidase on solid-state fermentation by Lichtheimia ramosa check for this species in other resources in agroindustrial residues: Characterization and catalytic properties of the enzymatic extract
Garcia, Nayara Fernanda Lisboa; da Silva Santos, Flávia Regina; Gonçalves, Fabiano Avelino; da Paz, Marcelo Fossa; Fonseca, Gustavo Graciano & Leite, Rodrigo Simões Ribeiro

Abstract

Background: β-Glucosidases catalyze the hydrolysis of cellobiose and cellodextrins, releasing glucose as the main product. This enzyme is used in the food, pharmaceutical, and biofuel industries. The aim of this work is to improve the β-glucosidase production by the fungus Lichtheimia ramosa check for this species in other resources by solid-state fermentation (SSF) using various agroindustrial residues and to evaluate the catalytic properties of this enzyme.
Results: A high production of β-glucosidase, about 274 U/g of dry substrate (or 27.4 U/mL), was obtained by cultivating the fungus on wheat bran with 65% of initial substrate moisture, at 96 h of incubation at 35°C. The enzymatic extract also exhibited carboxymethylcellulase (CMCase), xylanase, and β-xylosidase activities. The optimal activity of β-glucosidase was observed at pH 5.5 and 65°C and was stable over a pH range of 3.5–10.5. The enzyme maintained its activity (about 98% residual activity) after 1 h at 55°C. The enzyme was subject to reversible competitive inhibition with glucose and showed high catalytic activity in solutions containing up to 10% of ethanol.
Conclusions: β-Glucosidase characteristics associated with its ability to hydrolyze cellobiose, underscore the utility of this enzyme in diverse industrial processes.

Keywords
Cellobiase; Cellulases and hemicellulases; Industrial enzymes; Microbial enzymes

 
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