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Production of beta-glucosidase on solid-state fermentation by Lichtheimia ramosa in agroindustrial residues: characterization and catalytic properties of the enzymatic extract
Garcia, Nayara Fernanda Lisboa; Santos, Flávia Regina da Silva; Gonçalves, Fabiano Avelino; Paz, Marcelo Fossa da; Fonseca, Gustavo Graciano; Leite, Rodrigo Simões Ribeiro.
  • Garcia, Nayara Fernanda Lisboa; Universidade Federal da Grande Dourados. Faculdade de Ciências Biológicas e Ambientais. Laboratório de Enzimologia e Processos Fermentativos. Dourados. BR
  • Santos, Flávia Regina da Silva; Universidade Federal da Grande Dourados. Faculdade de Ciências Biológicas e Ambientais. Laboratório de Enzimologia e Processos Fermentativos. Dourados. BR
  • Gonçalves, Fabiano Avelino; Universidade Federal da Grande Dourados. Faculdade de Ciências Biológicas e Ambientais. Laboratório de Enzimologia e Processos Fermentativos. Dourados. BR
  • Paz, Marcelo Fossa da; Universidade Federal da Grande Dourados. Faculdade de Ciências Biológicas e Ambientais. Laboratório de Enzimologia e Processos Fermentativos. Dourados. BR
  • Fonseca, Gustavo Graciano; Universidade Federal da Grande Dourados. Faculdade de Ciências Biológicas e Ambientais. Laboratório de Enzimologia e Processos Fermentativos. Dourados. BR
  • Leite, Rodrigo Simões Ribeiro; Universidade Federal da Grande Dourados. Faculdade de Ciências Biológicas e Ambientais. Laboratório de Enzimologia e Processos Fermentativos. Dourados. BR
Electron. j. biotechnol ; 18(4): 314-319, July 2015. graf, tab
Article in English | LILACS | ID: lil-757870
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 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.
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Full text: Available Index: LILACS (Americas) Main subject: Beta-Glucosidase / Mucorales Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2015 Type: Article Affiliation country: Brazil Institution/Affiliation country: Universidade Federal da Grande Dourados/BR

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Full text: Available Index: LILACS (Americas) Main subject: Beta-Glucosidase / Mucorales Language: English Journal: Electron. j. biotechnol Journal subject: Biotechnology Year: 2015 Type: Article Affiliation country: Brazil Institution/Affiliation country: Universidade Federal da Grande Dourados/BR