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https://locus.ufv.br//handle/123456789/18128
Tipo: | Artigo |
Título: | Characteristics of free endoglucanase and glycosidases multienzyme complex from Fusarium verticillioides |
Autor(es): | Almeida, Maíra N.de Falkoski, Daniel L. Guimarães, Valéria M. Ramos, Humberto Josué de O. Visser, Evan M. Maitan-Alfenas, Gabriela P. Rezende, Sebastião T. de |
Abstract: | A novel multienzyme complex, E1 C , and a free endoglucanase, E2 (GH5), from Fusarium verticillioides were purified. The E1 C contained two endoglucanases (GH6 and GH10), one cellobiohydrolase (GH7) and one xylanase (GH10). Maximum activity was observed at 80 °C for both enzymes and they were thermostable at 50 and 60 °C. The activation energies for E1 C and E2 were 21.3 and 27.5 kJ/mol, respectively. The K M for E1 C was 10.25 g/L while for E2 was 6.58 g/L. Both E1 C and E2 were activated by Mn 2+ and CoCl 2 while they were inhibited by SDS, CuSO 4 , FeCl 3 , AgNO 4 , ZnSO 4 and HgCl 2 . E1 C and E2 presented endo-b-1,3–1,4-glucanase activity. E1 C presented crescent activity towards cellopentaose, cellotetraose and cellotriose. E2 hydrolyzed the substrates cellopentaose, cellotetraose and cellotriose with the same efficiency. E1 C showed a higher stability and a better hydrolysis performance than E2, suggesting advantages resulting from the physical interaction between proteins. |
Palavras-chave: | Multienzyme complex Endoglucanase Cellobiohydrolase Xylanase Fusarium verticillioides |
Editor: | Bioresource Technology |
Tipo de Acesso: | Published by Elsevier Ltd. |
URI: | https://doi.org/10.1016/j.biortech.2013.06.021 http://www.locus.ufv.br/handle/123456789/18128 |
Data do documento: | 8-Jun-2013 |
Aparece nas coleções: | Artigos |
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Arquivo | Descrição | Tamanho | Formato | |
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artigo.pdf Until 2100-12-31 | Texto completo | 1,05 MB | Adobe PDF | Visualizar/Abrir ACESSO RESTRITO |
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