Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Anais da Academia Brasileira de Ciências (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652021000600907 |
Resumo: | Abstract Solid state fermentation is a promising technology largely used in biotechnology process and is a suitable strategy for producing low-cost enzymatic products. At the present study, a novel enzyme obtained through solid state fermentation using Aspergillus sydowii was herein purified and characterized. The fermentations used coffee ground residue as substrate and the crude enzyme was submitted through further purification steps of: acetonic precipitation, DEAE-Sephadex and Superdex G-75 column. Both crude and purified enzymes were submitted to biochemical characterization of their thermostability, optimal temperature and pH, effects of inhibitors and metal ions. A purified protease was obtained with yield of 5.9-fold and 53% recovery, with maximal proteolytic activity of 352.0 U/mL. SDS-PAGE revealed a band of protein at 47.0 kDa. The enzyme activity was abolished in the presence of phenyl-methyl sulfonyl fluoride and partially inhibited against Triton X-100 (78.0%). The optimal activity was found in pH 8.0 at 45°C of temperature. Besides, the enzyme showed stability between 35°C and 50°C. It was possible to determine appropriate conditions to the obtainment of thermostable proteases with biotechnological interest associated with a method that concomitantly shows excellent production levels and recovery waste raw material in a very profitable process. |
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Anais da Academia Brasileira de Ciências (Online) |
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Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentationAspergillus sydowiibiotechnologyproteasessolid state fermentationwaste coffee residueAbstract Solid state fermentation is a promising technology largely used in biotechnology process and is a suitable strategy for producing low-cost enzymatic products. At the present study, a novel enzyme obtained through solid state fermentation using Aspergillus sydowii was herein purified and characterized. The fermentations used coffee ground residue as substrate and the crude enzyme was submitted through further purification steps of: acetonic precipitation, DEAE-Sephadex and Superdex G-75 column. Both crude and purified enzymes were submitted to biochemical characterization of their thermostability, optimal temperature and pH, effects of inhibitors and metal ions. A purified protease was obtained with yield of 5.9-fold and 53% recovery, with maximal proteolytic activity of 352.0 U/mL. SDS-PAGE revealed a band of protein at 47.0 kDa. The enzyme activity was abolished in the presence of phenyl-methyl sulfonyl fluoride and partially inhibited against Triton X-100 (78.0%). The optimal activity was found in pH 8.0 at 45°C of temperature. Besides, the enzyme showed stability between 35°C and 50°C. It was possible to determine appropriate conditions to the obtainment of thermostable proteases with biotechnological interest associated with a method that concomitantly shows excellent production levels and recovery waste raw material in a very profitable process.Academia Brasileira de Ciências2021-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652021000600907Anais da Academia Brasileira de Ciências v.93 suppl.3 2021reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765202120200867info:eu-repo/semantics/openAccessROCHA,FELYPE T.B.BRANDÃO-COSTA,ROMERO M.P.NEVES,ANNA GABRIELLY D.CARDOSO,KETHYLEN B.B.NASCIMENTO,THIAGO P.ALBUQUERQUE,WENDELL W.C.PORTO,ANA LÚCIA F.eng2021-09-22T00:00:00Zoai:scielo:S0001-37652021000600907Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2021-09-22T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false |
dc.title.none.fl_str_mv |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
title |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
spellingShingle |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation ROCHA,FELYPE T.B. Aspergillus sydowii biotechnology proteases solid state fermentation waste coffee residue |
title_short |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
title_full |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
title_fullStr |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
title_full_unstemmed |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
title_sort |
Purification and characterization of a protease from Aspergillus sydowii URM5774: Coffee ground residue for protease production by solid state fermentation |
author |
ROCHA,FELYPE T.B. |
author_facet |
ROCHA,FELYPE T.B. BRANDÃO-COSTA,ROMERO M.P. NEVES,ANNA GABRIELLY D. CARDOSO,KETHYLEN B.B. NASCIMENTO,THIAGO P. ALBUQUERQUE,WENDELL W.C. PORTO,ANA LÚCIA F. |
author_role |
author |
author2 |
BRANDÃO-COSTA,ROMERO M.P. NEVES,ANNA GABRIELLY D. CARDOSO,KETHYLEN B.B. NASCIMENTO,THIAGO P. ALBUQUERQUE,WENDELL W.C. PORTO,ANA LÚCIA F. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
ROCHA,FELYPE T.B. BRANDÃO-COSTA,ROMERO M.P. NEVES,ANNA GABRIELLY D. CARDOSO,KETHYLEN B.B. NASCIMENTO,THIAGO P. ALBUQUERQUE,WENDELL W.C. PORTO,ANA LÚCIA F. |
dc.subject.por.fl_str_mv |
Aspergillus sydowii biotechnology proteases solid state fermentation waste coffee residue |
topic |
Aspergillus sydowii biotechnology proteases solid state fermentation waste coffee residue |
description |
Abstract Solid state fermentation is a promising technology largely used in biotechnology process and is a suitable strategy for producing low-cost enzymatic products. At the present study, a novel enzyme obtained through solid state fermentation using Aspergillus sydowii was herein purified and characterized. The fermentations used coffee ground residue as substrate and the crude enzyme was submitted through further purification steps of: acetonic precipitation, DEAE-Sephadex and Superdex G-75 column. Both crude and purified enzymes were submitted to biochemical characterization of their thermostability, optimal temperature and pH, effects of inhibitors and metal ions. A purified protease was obtained with yield of 5.9-fold and 53% recovery, with maximal proteolytic activity of 352.0 U/mL. SDS-PAGE revealed a band of protein at 47.0 kDa. The enzyme activity was abolished in the presence of phenyl-methyl sulfonyl fluoride and partially inhibited against Triton X-100 (78.0%). The optimal activity was found in pH 8.0 at 45°C of temperature. Besides, the enzyme showed stability between 35°C and 50°C. It was possible to determine appropriate conditions to the obtainment of thermostable proteases with biotechnological interest associated with a method that concomitantly shows excellent production levels and recovery waste raw material in a very profitable process. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652021000600907 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652021000600907 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/0001-3765202120200867 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Academia Brasileira de Ciências |
publisher.none.fl_str_mv |
Academia Brasileira de Ciências |
dc.source.none.fl_str_mv |
Anais da Academia Brasileira de Ciências v.93 suppl.3 2021 reponame:Anais da Academia Brasileira de Ciências (Online) instname:Academia Brasileira de Ciências (ABC) instacron:ABC |
instname_str |
Academia Brasileira de Ciências (ABC) |
instacron_str |
ABC |
institution |
ABC |
reponame_str |
Anais da Academia Brasileira de Ciências (Online) |
collection |
Anais da Academia Brasileira de Ciências (Online) |
repository.name.fl_str_mv |
Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC) |
repository.mail.fl_str_mv |
||aabc@abc.org.br |
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1754302870557032448 |