Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
Purpose: In this study, an aqueous two-phase micellar system (ATPMS), formed by the non-ionic surfactant Triton X-114, was used to investigate the partitioning of cellulolytic enzymes produced by the filamentous fungus Aspergillus fumigatus CCT 7873. Methods: Performance of the ATPMS on the partitio...
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| Principais autores: | , , , , |
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| Formato: | article |
| Idioma: | English |
| Publicado em: |
Annals of Microbiology
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| Endereço do item: | https://repositorio.ufrn.br/handle/123456789/32311 |
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| Resumo: | Purpose: In this study, an aqueous two-phase micellar system (ATPMS), formed by the non-ionic surfactant Triton X-114, was used to investigate the partitioning of cellulolytic enzymes produced by the filamentous fungus Aspergillus fumigatus CCT 7873. Methods: Performance of the ATPMS on the partitioning of CMCase (activity on carboxymethyl cellulose) and FPase (activity on filter paper) was investigated by varying the temperature (35, 40, 45, 50, 55, 60, and 65 °C), enzyme crude extract concentration (20, 40, 60, and 80% w/w), and Triton X-114 concentration (2, 4, 6, and 8% w/w) and by adding different inorganic salts (NaCl, CaCl2, MgSO4, and MnSO4) in the system. Results: An ATPMS formed with 8% (w/w) Triton X-114 and 40% (w/w) enzymatic crude extract at a system temperature of 55 °C was most favorable for partitioning the tested enzymes. Under these conditions, a purification factor for CMCase and FPase of 10.89 and 0.65 was reached, respectively. The addition of inorganic salts changed the distribution of enzymes. Of these, CaCl2 contributed to a higher distribution coefficient (50.0), whereas for FPase, the presence of MnSO4 in the system improved the purification factor to 3.94. Conclusion: The highest values obtained for the yield and purification factors demonstrate that ATPMS is an interesting option for recovering and purifying cellulolytic enzymes |
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