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Streptomyces misionensis PESB-25 Produces a Thermoacidophilic Endoglucanase Using Sugarcane Bagasse and Corn Steep Liquor as the Sole Organic Substrates

Streptomyces misionensis strain PESB-25 was screened and selected for its ability to secrete cellulases. Cells were grown in a liquid medium containing sugarcane bagasse (SCB) as carbon source and corn steep liquor (CSL) as nitrogen source, whose concentrations were optimized using response surface...

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Detalles Bibliográficos
Autores principales: Franco-Cirigliano, Marcella Novaes, Rezende, Raquel de Carvalho, Gravina-Oliveira, Mônica Pires, Pereira, Pedro Henrique Freitas, do Nascimento, Rodrigo Pires, Bon, Elba Pinto da Silva, Macrae, Andrew, Coelho, Rosalie Reed Rodrigues
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3622310/
https://www.ncbi.nlm.nih.gov/pubmed/23586048
http://dx.doi.org/10.1155/2013/584207
Descripción
Sumario:Streptomyces misionensis strain PESB-25 was screened and selected for its ability to secrete cellulases. Cells were grown in a liquid medium containing sugarcane bagasse (SCB) as carbon source and corn steep liquor (CSL) as nitrogen source, whose concentrations were optimized using response surface methodology (RSM). A peak of endoglucanase accumulation (1.01 U·mL(−1)) was observed in a medium with SCB 1.0% (w/v) and CSL 1.2% (w/v) within three days of cultivation. S. misionensis PESB-25 endoglucanase activity was thermoacidophilic with optimum pH and temperature range of 3.0 to 3.6 and 62° to 70°C, respectively. In these conditions, values of 1.54 U mL(−1) of endoglucanase activity were observed. Moreover, Mn(2+) was demonstrated to have a hyperactivating effect on the enzyme. In the presence of MnSO(4) (8 mM), the enzyme activity increased threefold, up to 4.34 U·mL(−1). Mn(2+) also improved endoglucanase stability as the catalyst retained almost full activity upon incubation at 50°C for 4 h, while in the absence of Mn(2+), enzyme activity decreased by 50% in this same period. Three protein bands with endoglucanase activity and apparent molecular masses of 12, 48.5 and 119.5 kDa were detected by zymogram.