Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s13205-018-1397-6 http://hdl.handle.net/11449/160489 |
Resumo: | The filamentous fungus Aspergillus niveus produced extracellular antifungal chitinase when cultured under submerged fermentation (SbmF) using crab shells as the carbon source. Maximal chitinase production was achieved at 192 h of cultivation using minimal medium containing 1% chitin. The enzyme was purified 1.97-fold with 40% recovery by ammonium sulfate precipitation and Sephadex G-100 gel filtration. The molecular mass was estimated to be 44 kDa by both 12% SDS-PAGE and Sepharose CL-6B gel filtration. Maximal A. niveus chitinase activity was obtained at 65 degrees C and pH 5.0. The enzyme was fully stable at 60 degrees C for up to 120 min and the enzymatic activity was increased by Mn2+. In the presence of reducing and denaturing compounds, the enzyme activity was not drastically affected. The chitinase was able to hydrolyze colloidal chitin, azure chitin, and 4-nitrophenyl N-acetyl-beta-D glucosaminide; for the latter, the K-0.5 and maximal velocity (V-max) were 3.51 mM and 9.68 U/mg of protein, respectively. The A. niveus chitinase presented antifungal activity against Aspergillus niger (MIC = 84 mu g/mL), A. fumigatus (MIC = 21 mu g/mL), A. flavus (MIC = 24 mu g/mL), A. phoenicis (MIC = 24 mu g/mL), and Paecilomyces variotii (MIC = 21 mu g/mL). The fungus A. niveus was able to produce a thermostable and denaturation-resistant chitinase able to inhibit fungal development, signaling its biotechnological potential. |
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Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentationAspergillus niveusAntifungal activityChitinChitinaseFungal hydrolasesThe filamentous fungus Aspergillus niveus produced extracellular antifungal chitinase when cultured under submerged fermentation (SbmF) using crab shells as the carbon source. Maximal chitinase production was achieved at 192 h of cultivation using minimal medium containing 1% chitin. The enzyme was purified 1.97-fold with 40% recovery by ammonium sulfate precipitation and Sephadex G-100 gel filtration. The molecular mass was estimated to be 44 kDa by both 12% SDS-PAGE and Sepharose CL-6B gel filtration. Maximal A. niveus chitinase activity was obtained at 65 degrees C and pH 5.0. The enzyme was fully stable at 60 degrees C for up to 120 min and the enzymatic activity was increased by Mn2+. In the presence of reducing and denaturing compounds, the enzyme activity was not drastically affected. The chitinase was able to hydrolyze colloidal chitin, azure chitin, and 4-nitrophenyl N-acetyl-beta-D glucosaminide; for the latter, the K-0.5 and maximal velocity (V-max) were 3.51 mM and 9.68 U/mg of protein, respectively. The A. niveus chitinase presented antifungal activity against Aspergillus niger (MIC = 84 mu g/mL), A. fumigatus (MIC = 21 mu g/mL), A. flavus (MIC = 24 mu g/mL), A. phoenicis (MIC = 24 mu g/mL), and Paecilomyces variotii (MIC = 21 mu g/mL). The fungus A. niveus was able to produce a thermostable and denaturation-resistant chitinase able to inhibit fungal development, signaling its biotechnological potential.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Univ Estadual Paulista, Inst Quim, Rua Prof Francisco Degni 55, BR-14800900 Araraquara, SP, BrazilUniv Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP, BrazilUniv Estadual Paulista, Inst Quim, Rua Prof Francisco Degni 55, BR-14800900 Araraquara, SP, BrazilFAPESP: 2011/50880-1SpringerUniversidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Alves, Thais Barboni [UNESP]Oliveira Ornela, Pedro Henrique de [UNESP]Cavalcanti de Oliveira, Arthur Henrique [UNESP]Jorge, Joao AtilioSouza Guimaraes, Luis Henrique [UNESP]2018-11-26T16:04:41Z2018-11-26T16:04:41Z2018-08-10info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10http://dx.doi.org/10.1007/s13205-018-1397-63 Biotech. Heidelberg: Springer Heidelberg, v. 8, n. 8, 10 p., 2018.2190-572Xhttp://hdl.handle.net/11449/16048910.1007/s13205-018-1397-6WOS:000441262700004Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPeng3 Biotechinfo:eu-repo/semantics/openAccess2021-10-23T12:40:10Zoai:repositorio.unesp.br:11449/160489Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T12:40:10Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
title |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
spellingShingle |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation Alves, Thais Barboni [UNESP] Aspergillus niveus Antifungal activity Chitin Chitinase Fungal hydrolases |
title_short |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
title_full |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
title_fullStr |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
title_full_unstemmed |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
title_sort |
Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation |
author |
Alves, Thais Barboni [UNESP] |
author_facet |
Alves, Thais Barboni [UNESP] Oliveira Ornela, Pedro Henrique de [UNESP] Cavalcanti de Oliveira, Arthur Henrique [UNESP] Jorge, Joao Atilio Souza Guimaraes, Luis Henrique [UNESP] |
author_role |
author |
author2 |
Oliveira Ornela, Pedro Henrique de [UNESP] Cavalcanti de Oliveira, Arthur Henrique [UNESP] Jorge, Joao Atilio Souza Guimaraes, Luis Henrique [UNESP] |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Alves, Thais Barboni [UNESP] Oliveira Ornela, Pedro Henrique de [UNESP] Cavalcanti de Oliveira, Arthur Henrique [UNESP] Jorge, Joao Atilio Souza Guimaraes, Luis Henrique [UNESP] |
dc.subject.por.fl_str_mv |
Aspergillus niveus Antifungal activity Chitin Chitinase Fungal hydrolases |
topic |
Aspergillus niveus Antifungal activity Chitin Chitinase Fungal hydrolases |
description |
The filamentous fungus Aspergillus niveus produced extracellular antifungal chitinase when cultured under submerged fermentation (SbmF) using crab shells as the carbon source. Maximal chitinase production was achieved at 192 h of cultivation using minimal medium containing 1% chitin. The enzyme was purified 1.97-fold with 40% recovery by ammonium sulfate precipitation and Sephadex G-100 gel filtration. The molecular mass was estimated to be 44 kDa by both 12% SDS-PAGE and Sepharose CL-6B gel filtration. Maximal A. niveus chitinase activity was obtained at 65 degrees C and pH 5.0. The enzyme was fully stable at 60 degrees C for up to 120 min and the enzymatic activity was increased by Mn2+. In the presence of reducing and denaturing compounds, the enzyme activity was not drastically affected. The chitinase was able to hydrolyze colloidal chitin, azure chitin, and 4-nitrophenyl N-acetyl-beta-D glucosaminide; for the latter, the K-0.5 and maximal velocity (V-max) were 3.51 mM and 9.68 U/mg of protein, respectively. The A. niveus chitinase presented antifungal activity against Aspergillus niger (MIC = 84 mu g/mL), A. fumigatus (MIC = 21 mu g/mL), A. flavus (MIC = 24 mu g/mL), A. phoenicis (MIC = 24 mu g/mL), and Paecilomyces variotii (MIC = 21 mu g/mL). The fungus A. niveus was able to produce a thermostable and denaturation-resistant chitinase able to inhibit fungal development, signaling its biotechnological potential. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-11-26T16:04:41Z 2018-11-26T16:04:41Z 2018-08-10 |
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/10.1007/s13205-018-1397-6 3 Biotech. Heidelberg: Springer Heidelberg, v. 8, n. 8, 10 p., 2018. 2190-572X http://hdl.handle.net/11449/160489 10.1007/s13205-018-1397-6 WOS:000441262700004 |
url |
http://dx.doi.org/10.1007/s13205-018-1397-6 http://hdl.handle.net/11449/160489 |
identifier_str_mv |
3 Biotech. Heidelberg: Springer Heidelberg, v. 8, n. 8, 10 p., 2018. 2190-572X 10.1007/s13205-018-1397-6 WOS:000441262700004 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
3 Biotech |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
10 |
dc.publisher.none.fl_str_mv |
Springer |
publisher.none.fl_str_mv |
Springer |
dc.source.none.fl_str_mv |
Web of Science 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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1799965447013007360 |