Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system

Detalhes bibliográficos
Autor(a) principal: Santos, Everaldo Silvino dos
Data de Publicação: 2020
Outros Autores: Oliveira Júnior, Sérgio Dantas de, Padilha, Carlos Eduardo de Araújo, Asevedo, Estefani Alves de, Macedo, Gorete Ribeiro de
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UFRN
Texto Completo: https://repositorio.ufrn.br/handle/123456789/32311
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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spelling Santos, Everaldo Silvino dosOliveira Júnior, Sérgio Dantas dePadilha, Carlos Eduardo de AraújoAsevedo, Estefani Alves deMacedo, Gorete Ribeiro de2021-04-26T13:31:43Z2021-04-26T13:31:43Z2020-05-04OLIVEIRA JÚNIOR, S.D.; PADILHA, C.E.A.; ASEVEDO, E.A.; MACEDO, G.R.; SANTOS, E.S.. Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system. Annals of Microbiology, v. 70, p. 23, 2020. Disponível em https://annalsmicrobiology.biomedcentral.com/articles/10.1186/s13213-020-01573-w. Acesso em 30 mar. 2021. https://doi.org/10.1186/s13213-020-01573-w1590-42611869-2044https://repositorio.ufrn.br/handle/123456789/3231110.1186/s13213-020-01573-wAnnals of MicrobiologyAttribution 3.0 Brazilhttp://creativecommons.org/licenses/by/3.0/br/info:eu-repo/semantics/openAccessAspergillus fumigatusCellulasesMicellesLiquid-liquid extractionDownstream processingRecovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar systeminfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlePurpose: 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 enzymesengreponame:Repositório Institucional da UFRNinstname:Universidade Federal do Rio Grande do Norte (UFRN)instacron:UFRNORIGINALRecoveryAndPurification_Santos_2020.pdfRecoveryAndPurification_Santos_2020.pdfapplication/pdf2269452https://repositorio.ufrn.br/bitstream/123456789/32311/1/RecoveryAndPurification_Santos_2020.pdfc748eaae56e758d494adc8d475c47d54MD51CC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8914https://repositorio.ufrn.br/bitstream/123456789/32311/2/license_rdf4d2950bda3d176f570a9f8b328dfbbefMD52LICENSElicense.txtlicense.txttext/plain; charset=utf-81484https://repositorio.ufrn.br/bitstream/123456789/32311/3/license.txte9597aa2854d128fd968be5edc8a28d9MD53TEXTRecoveryAndPurification_Santos_2020.pdf.txtRecoveryAndPurification_Santos_2020.pdf.txtExtracted texttext/plain40078https://repositorio.ufrn.br/bitstream/123456789/32311/4/RecoveryAndPurification_Santos_2020.pdf.txta49cec372cd7b5544404e578620dc0b1MD54THUMBNAILRecoveryAndPurification_Santos_2020.pdf.jpgRecoveryAndPurification_Santos_2020.pdf.jpgGenerated Thumbnailimage/jpeg1812https://repositorio.ufrn.br/bitstream/123456789/32311/5/RecoveryAndPurification_Santos_2020.pdf.jpg5bedc27714821884180a7e4a1dc44f85MD55123456789/323112021-05-02 08:35:31.728oai:https://repositorio.ufrn.br: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Repositório de PublicaçõesPUBhttp://repositorio.ufrn.br/oai/opendoar:2021-05-02T11:35:31Repositório Institucional da UFRN - Universidade Federal do Rio Grande do Norte (UFRN)false
dc.title.pt_BR.fl_str_mv Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
title Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
spellingShingle Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
Santos, Everaldo Silvino dos
Aspergillus fumigatus
Cellulases
Micelles
Liquid-liquid extraction
Downstream processing
title_short Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
title_full Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
title_fullStr Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
title_full_unstemmed Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
title_sort Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system
author Santos, Everaldo Silvino dos
author_facet Santos, Everaldo Silvino dos
Oliveira Júnior, Sérgio Dantas de
Padilha, Carlos Eduardo de Araújo
Asevedo, Estefani Alves de
Macedo, Gorete Ribeiro de
author_role author
author2 Oliveira Júnior, Sérgio Dantas de
Padilha, Carlos Eduardo de Araújo
Asevedo, Estefani Alves de
Macedo, Gorete Ribeiro de
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Santos, Everaldo Silvino dos
Oliveira Júnior, Sérgio Dantas de
Padilha, Carlos Eduardo de Araújo
Asevedo, Estefani Alves de
Macedo, Gorete Ribeiro de
dc.subject.por.fl_str_mv Aspergillus fumigatus
Cellulases
Micelles
Liquid-liquid extraction
Downstream processing
topic Aspergillus fumigatus
Cellulases
Micelles
Liquid-liquid extraction
Downstream processing
description 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
publishDate 2020
dc.date.issued.fl_str_mv 2020-05-04
dc.date.accessioned.fl_str_mv 2021-04-26T13:31:43Z
dc.date.available.fl_str_mv 2021-04-26T13:31:43Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.citation.fl_str_mv OLIVEIRA JÚNIOR, S.D.; PADILHA, C.E.A.; ASEVEDO, E.A.; MACEDO, G.R.; SANTOS, E.S.. Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system. Annals of Microbiology, v. 70, p. 23, 2020. Disponível em https://annalsmicrobiology.biomedcentral.com/articles/10.1186/s13213-020-01573-w. Acesso em 30 mar. 2021. https://doi.org/10.1186/s13213-020-01573-w
dc.identifier.uri.fl_str_mv https://repositorio.ufrn.br/handle/123456789/32311
dc.identifier.issn.none.fl_str_mv 1590-4261
1869-2044
dc.identifier.doi.none.fl_str_mv 10.1186/s13213-020-01573-w
identifier_str_mv OLIVEIRA JÚNIOR, S.D.; PADILHA, C.E.A.; ASEVEDO, E.A.; MACEDO, G.R.; SANTOS, E.S.. Recovery and purification of cellulolytic enzymes from Aspergillus fumigatus CCT 7873 using an aqueous two-phase micellar system. Annals of Microbiology, v. 70, p. 23, 2020. Disponível em https://annalsmicrobiology.biomedcentral.com/articles/10.1186/s13213-020-01573-w. Acesso em 30 mar. 2021. https://doi.org/10.1186/s13213-020-01573-w
1590-4261
1869-2044
10.1186/s13213-020-01573-w
url https://repositorio.ufrn.br/handle/123456789/32311
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv Attribution 3.0 Brazil
http://creativecommons.org/licenses/by/3.0/br/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Attribution 3.0 Brazil
http://creativecommons.org/licenses/by/3.0/br/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Annals of Microbiology
publisher.none.fl_str_mv Annals of Microbiology
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