Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , |
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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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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1792961660970860544 |