Streptomyces misionensisPESB-25 Produces a Thermoacidophilic Endoglucanase Using Sugarcane Bagasse and Corn Steep Liquor as the Sole Organic Substrates
| Autor: | Andrew Macrae, Raquel de Carvalho Rezende, Mônica Pires Gravina-Oliveira, Marcella Novaes Franco-Cirigliano, Elba P. S. Bon, Pedro Henrique Freitas Pereira, Rosalie Reed Rodrigues Coelho, Rodrigo Pires do Nascimento |
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| Rok vydání: | 2013 |
| Předmět: |
Article Subject
Nitrogen lcsh:Medicine Cellulase Zea mays Corn steep liquor Streptomyces General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Enzyme Stability Botany Food science Cellulose General Immunology and Microbiology biology lcsh:R Temperature General Medicine Streptomyces misionensis Hydrogen-Ion Concentration biology.organism_classification Carbon Enzyme assay Culture Media Saccharum chemistry Fermentation biology.protein Bagasse Research Article |
| Zdroj: | BioMed Research International BioMed Research International, Vol 2013 (2013) |
| ISSN: | 2314-6141 2314-6133 |
| DOI: | 10.1155/2013/584207 |
| Popis: | Streptomyces misionensisstrain 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. misionensisPESB-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−1of endoglucanase activity were observed. Moreover, Mn2+was demonstrated to have a hyperactivating effect on the enzyme. In the presence of MnSO4(8 mM), the enzyme activity increased threefold, up to 4.34 U·mL−1. Mn2+also improved endoglucanase stability as the catalyst retained almost full activity upon incubation at 50°C for 4 h, while in the absence of Mn2+, 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. |
| Databáze: | OpenAIRE |
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