Characteristics of free endoglucanase and glycosidases multienzyme complex from Fusarium verticillioides
| Autor: | Sebastião Tavares de Rezende, Humberto J.O. Ramos, Maíra Nicolau de Almeida, Evan Michael Visser, Daniel Luciano Falkoski, Valéria Monteze Guimarães, Gabriela Piccolo Maitan-Alfenas |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Fusarium
Environmental Engineering Glycoside Hydrolases Stereochemistry Molecular Sequence Data Bioengineering Cellulase Fusarium verticillioides Mass Spectrometry Microbiology Substrate Specificity chemistry.chemical_compound Hydrolysis Multienzyme Complexes Glycoside hydrolase Amino Acid Sequence Cellulose Endoglucanase Enzyme Inhibitors Waste Management and Disposal Peptide sequence chemistry.chemical_classification biology Renewable Energy Sustainability and the Environment Xylanase Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Multienzyme complex Molecular Weight Kinetics Enzyme chemistry biology.protein Cellobiohydrolase Electrophoresis Polyacrylamide Gel |
| Zdroj: | LOCUS Repositório Institucional da UFV Universidade Federal de Viçosa (UFV) instacron:UFV |
| ISSN: | 1873-2976 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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