Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum

Detalhes bibliográficos
Autor(a) principal: Ida, Érika Lika
Data de Publicação: 2017
Outros Autores: da Silva, Ronivaldo Rodrigues [UNESP], de Oliveira, Tássio Brito [UNESP], Souto, Tatiane Beltramini, Leite, Juliana Abigail, Rodrigues, André [UNESP], Cabral, Hamilton
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1080/10826068.2016.1224247
http://hdl.handle.net/11449/173776
Resumo: Filamentous fungi secrete diverse peptidases with different biochemical properties, which is of considerable importance for application in various commercial sectors. In this study, we describe the isolation of two fungal species collected from the soil of decayed organic matter: Aspergillus fischeri and Penicillium citrinum. In a submerged bioprocess, we observed better peptidase production with the fungus P. citrinum, which reached a peak production at 168 h with 760 U/mL, in comparison with the fungus A. fischeri, which reached a peak production at 72 h with 460 U/mL. In both situations, the fermentative medium contained 0.5% crushed feathers as a source of nitrogen. On performing biochemical characterization, we detected two alkaline serine peptidases: The one secreted by P. citrinum had optimal activity at pH 7.0 and at 45°C, while the one secreted by A. fischeri had optimal activity in pH 6.5–8 and at 55–60°C. Metallic ions were effective in modulating these peptidases; in particular, Cu2+ promoted negative modulation of both peptidases. The peptidases were stable and functional under conditions of nonionic surfactants, temperatures up to 45°C for 1 h, and incubation over a wide pH range. In addition, it was observed that both peptidases had the capacity to hydrolyze collagen and performed well in removing an egg protein stain when supplemented into a commercial powder detergent; this was especially true for the peptidase from P. citrinum.
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spelling Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinumBiochemical characterizationcrude enzyme extractprotease applicationproteasessubmerged fermentationFilamentous fungi secrete diverse peptidases with different biochemical properties, which is of considerable importance for application in various commercial sectors. In this study, we describe the isolation of two fungal species collected from the soil of decayed organic matter: Aspergillus fischeri and Penicillium citrinum. In a submerged bioprocess, we observed better peptidase production with the fungus P. citrinum, which reached a peak production at 168 h with 760 U/mL, in comparison with the fungus A. fischeri, which reached a peak production at 72 h with 460 U/mL. In both situations, the fermentative medium contained 0.5% crushed feathers as a source of nitrogen. On performing biochemical characterization, we detected two alkaline serine peptidases: The one secreted by P. citrinum had optimal activity at pH 7.0 and at 45°C, while the one secreted by A. fischeri had optimal activity in pH 6.5–8 and at 55–60°C. Metallic ions were effective in modulating these peptidases; in particular, Cu2+ promoted negative modulation of both peptidases. The peptidases were stable and functional under conditions of nonionic surfactants, temperatures up to 45°C for 1 h, and incubation over a wide pH range. In addition, it was observed that both peptidases had the capacity to hydrolyze collagen and performed well in removing an egg protein stain when supplemented into a commercial powder detergent; this was especially true for the peptidase from P. citrinum.Department of Pharmaceutical Sciences School of Pharmaceutical Sciences of Ribeirao Preto University of Sao PauloDepartment of Biology Institute of Biosciences Letters and Exact Sciences Sao Paulo State University UNESP/IBILCEDepartment of Biochemistry and Microbiology Sao Paulo State University UNESPDepartment of Biology Institute of Biosciences Letters and Exact Sciences Sao Paulo State University UNESP/IBILCEDepartment of Biochemistry and Microbiology Sao Paulo State University UNESPUniversidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Ida, Érika Likada Silva, Ronivaldo Rodrigues [UNESP]de Oliveira, Tássio Brito [UNESP]Souto, Tatiane BeltraminiLeite, Juliana AbigailRodrigues, André [UNESP]Cabral, Hamilton2018-12-11T17:07:43Z2018-12-11T17:07:43Z2017-03-16info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article282-290application/pdfhttp://dx.doi.org/10.1080/10826068.2016.1224247Preparative Biochemistry and Biotechnology, v. 47, n. 3, p. 282-290, 2017.1532-22971082-6068http://hdl.handle.net/11449/17377610.1080/10826068.2016.12242472-s2.0-849948024112-s2.0-84994802411.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPreparative Biochemistry and Biotechnology0,3620,362info:eu-repo/semantics/openAccess2023-10-27T06:07:00Zoai:repositorio.unesp.br:11449/173776Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-10-27T06:07Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
title Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
spellingShingle Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
Ida, Érika Lika
Biochemical characterization
crude enzyme extract
protease application
proteases
submerged fermentation
title_short Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
title_full Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
title_fullStr Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
title_full_unstemmed Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
title_sort Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
author Ida, Érika Lika
author_facet Ida, Érika Lika
da Silva, Ronivaldo Rodrigues [UNESP]
de Oliveira, Tássio Brito [UNESP]
Souto, Tatiane Beltramini
Leite, Juliana Abigail
Rodrigues, André [UNESP]
Cabral, Hamilton
author_role author
author2 da Silva, Ronivaldo Rodrigues [UNESP]
de Oliveira, Tássio Brito [UNESP]
Souto, Tatiane Beltramini
Leite, Juliana Abigail
Rodrigues, André [UNESP]
Cabral, Hamilton
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de São Paulo (USP)
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Ida, Érika Lika
da Silva, Ronivaldo Rodrigues [UNESP]
de Oliveira, Tássio Brito [UNESP]
Souto, Tatiane Beltramini
Leite, Juliana Abigail
Rodrigues, André [UNESP]
Cabral, Hamilton
dc.subject.por.fl_str_mv Biochemical characterization
crude enzyme extract
protease application
proteases
submerged fermentation
topic Biochemical characterization
crude enzyme extract
protease application
proteases
submerged fermentation
description Filamentous fungi secrete diverse peptidases with different biochemical properties, which is of considerable importance for application in various commercial sectors. In this study, we describe the isolation of two fungal species collected from the soil of decayed organic matter: Aspergillus fischeri and Penicillium citrinum. In a submerged bioprocess, we observed better peptidase production with the fungus P. citrinum, which reached a peak production at 168 h with 760 U/mL, in comparison with the fungus A. fischeri, which reached a peak production at 72 h with 460 U/mL. In both situations, the fermentative medium contained 0.5% crushed feathers as a source of nitrogen. On performing biochemical characterization, we detected two alkaline serine peptidases: The one secreted by P. citrinum had optimal activity at pH 7.0 and at 45°C, while the one secreted by A. fischeri had optimal activity in pH 6.5–8 and at 55–60°C. Metallic ions were effective in modulating these peptidases; in particular, Cu2+ promoted negative modulation of both peptidases. The peptidases were stable and functional under conditions of nonionic surfactants, temperatures up to 45°C for 1 h, and incubation over a wide pH range. In addition, it was observed that both peptidases had the capacity to hydrolyze collagen and performed well in removing an egg protein stain when supplemented into a commercial powder detergent; this was especially true for the peptidase from P. citrinum.
publishDate 2017
dc.date.none.fl_str_mv 2017-03-16
2018-12-11T17:07:43Z
2018-12-11T17:07:43Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1080/10826068.2016.1224247
Preparative Biochemistry and Biotechnology, v. 47, n. 3, p. 282-290, 2017.
1532-2297
1082-6068
http://hdl.handle.net/11449/173776
10.1080/10826068.2016.1224247
2-s2.0-84994802411
2-s2.0-84994802411.pdf
url http://dx.doi.org/10.1080/10826068.2016.1224247
http://hdl.handle.net/11449/173776
identifier_str_mv Preparative Biochemistry and Biotechnology, v. 47, n. 3, p. 282-290, 2017.
1532-2297
1082-6068
10.1080/10826068.2016.1224247
2-s2.0-84994802411
2-s2.0-84994802411.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Preparative Biochemistry and Biotechnology
0,362
0,362
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 282-290
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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