Characterization of the cellulase-secretome produced by the Antarctic bacterium Flavobacterium sp. AUG42
| Autor: | Victoria Braña, Lorena M. Herrera, Laura Franco Fraguas, Susana Castro-Sowinski |
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| Přispěvatelé: | Herrera Lorena, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología., Braña Victoria, IIBCE, Franco-Fraguas Laura, Universidad de la República (Uruguay). Facultad de Química., Castro-Sowinski Susana, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Glycoside Hydrolases Antarctic Regions Cellulase Bacterial growth Saccharification Microbiology Flavobacterium Carbon Cycle Substrate Specificity 03 medical and health sciences Hydrolysis Catalytic Domain Cellulases Glycoside hydrolase Cellulose Enzyme Assays 030304 developmental biology chemistry.chemical_classification 0303 health sciences Base Sequence biology 030306 microbiology beta-Glucosidase Temperature Glycoside Carbon cycle Hydrogen-Ion Concentration Carbohydrate biology.organism_classification Carbon Kinetics Glucose chemistry Biochemistry Carboxymethylcellulose Sodium Fermentation biology.protein Antarctica Bacteria |
| Zdroj: | COLIBRI Universidad de la República instacron:Universidad de la República |
| Popis: | Flavobacterium sp. AUG42 is a cellulase-producing bacterium isolated from the Antarctic oligochaete Grania sp. (Annelida). In this work, we report that AUG42 produces a glycoside hydrolase cocktail with CMCase, PASCase and cellobiase activities (optimum pHs and temperatures ranging from 5.5 to 6.5 and 40 to 50 °C, respectively). The time-course analyses of the bacterial growth and cellulase production showed that the cocktail has maximal activity at the stationary phase when growing at 16 °C with filter paper as a cellulosic carbon source, among the tested substrates. The analyses of the CAZome and the identification of secreted proteins by shotgun Mass Spectrometry analysis showed that five glycoside hydrolyses are present in the bacterial secretome, which probably cooperate in the degradation of the cellulosic substrates. Two of these glycoside hydrolyses may harbor putative carbohydrate binding modules, both with a cleft-like active site. The cellulolytic cocktail was assayed in saccharification experiments using carboxymethylcellulose as a substrate and results showed the release of glucose (a fermentable sugar) and other reducing-sugars, after 24 h incubation. The ecological relevance of producing cellulases in the Antarctic environment, as well as their potential use in the bio-refinery industry, are discussed. |
| Databáze: | OpenAIRE |
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