Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.ejbt.2015.09.008 http://hdl.handle.net/11449/158592 |
Resumo: | Background: Tannases are enzymes with biotechnological potential produced mainly by microorganisms as filamentous fungi. In this context, the production and characterization of a multi-tolerant tannase from Aspergillus carbonarius is described. Results: The filamentous fungus A. carbonarius produced high levels of tannase when cultivated under solid-state fermentation using green tea leaves as substrate/carbon source and tapwater at a 1:1 ratio as the moisture agent for 72 h at 30 degrees C. Two tannase activity peakswere obtained during the purification step using DEAE-Cellulose. The second peak (peak II) was purified 11-fold with 14% recovery from a Sepharose CL-6B chromatographic column. The tannase from peak II (tannase II) was characterized as a heterodimeric glycoprotein of 134.89 kDa, estimated through gel filtration, with subunits of 65 kDa and 100 kDa, estimated through SDS-PAGE, and 48% carbohydrate content. The optimal temperature and pH for tannase II activity was 60 degrees C and 5.0, respectively. The enzyme was fully stable at temperatures ranging from 20-60 degrees C for 120 min, and the half-life (T1/2) at 75 degrees C was 62 min. The activation energy was 28.93 kJ/mol. After incubation at pH 5.0 for 60 min, 75% of the enzyme activity was maintained. However, enzyme activity was increased in the presence of AgNO3 and it was tolerant to solvents and detergents. Tannase II exhibited a better affinity for methyl gallate (Km = 1.42 mM) rather than for tannic acid (Km = 2.2 mM). Conclusion: A. carbonarius tannase presented interesting properties as, for example, multi-tolerance, which highlight its potential for future application. (C) 2015 Pontificia Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. All rights reserved. |
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Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentationAspergillusMicrobial enzymesSolid-state fermentationTannaseTannic acidBackground: Tannases are enzymes with biotechnological potential produced mainly by microorganisms as filamentous fungi. In this context, the production and characterization of a multi-tolerant tannase from Aspergillus carbonarius is described. Results: The filamentous fungus A. carbonarius produced high levels of tannase when cultivated under solid-state fermentation using green tea leaves as substrate/carbon source and tapwater at a 1:1 ratio as the moisture agent for 72 h at 30 degrees C. Two tannase activity peakswere obtained during the purification step using DEAE-Cellulose. The second peak (peak II) was purified 11-fold with 14% recovery from a Sepharose CL-6B chromatographic column. The tannase from peak II (tannase II) was characterized as a heterodimeric glycoprotein of 134.89 kDa, estimated through gel filtration, with subunits of 65 kDa and 100 kDa, estimated through SDS-PAGE, and 48% carbohydrate content. The optimal temperature and pH for tannase II activity was 60 degrees C and 5.0, respectively. The enzyme was fully stable at temperatures ranging from 20-60 degrees C for 120 min, and the half-life (T1/2) at 75 degrees C was 62 min. The activation energy was 28.93 kJ/mol. After incubation at pH 5.0 for 60 min, 75% of the enzyme activity was maintained. However, enzyme activity was increased in the presence of AgNO3 and it was tolerant to solvents and detergents. Tannase II exhibited a better affinity for methyl gallate (Km = 1.42 mM) rather than for tannic acid (Km = 2.2 mM). Conclusion: A. carbonarius tannase presented interesting properties as, for example, multi-tolerance, which highlight its potential for future application. (C) 2015 Pontificia Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Univ Estadual Paulista, Inst Quim Araraquara, BR-14800900 Sao Paulo, BrazilUniv Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Pret, Dept Biol, BR-14040901 Sao Paulo, BrazilUniv Estadual Paulista, Inst Quim Araraquara, BR-14800900 Sao Paulo, BrazilFAPESP: 2011/50880-1Univ Catolica De ValparaisoUniversidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Valera, Larissa Serrani [UNESP]Jorge, Joao AtilioSouza Guimaraes, Luis Henrique2018-11-26T15:28:14Z2018-11-26T15:28:14Z2015-11-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article464-470application/pdfhttp://dx.doi.org/10.1016/j.ejbt.2015.09.008Electronic Journal Of Biotechnology. Valparaiso: Univ Catolica De Valparaiso, v. 18, n. 6, p. 464-470, 2015.0717-3458http://hdl.handle.net/11449/15859210.1016/j.ejbt.2015.09.008WOS:000365070500013WOS000365070500013.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengElectronic Journal Of Biotechnology0,537info:eu-repo/semantics/openAccess2023-10-18T06:08:50Zoai:repositorio.unesp.br:11449/158592Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:15:21.138729Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
title |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
spellingShingle |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation Valera, Larissa Serrani [UNESP] Aspergillus Microbial enzymes Solid-state fermentation Tannase Tannic acid |
title_short |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
title_full |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
title_fullStr |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
title_full_unstemmed |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
title_sort |
Characterization of a multi-tolerant tannin acyl hydrolase II from Aspergillus carbonarius produced under solid-state fermentation |
author |
Valera, Larissa Serrani [UNESP] |
author_facet |
Valera, Larissa Serrani [UNESP] Jorge, Joao Atilio Souza Guimaraes, Luis Henrique |
author_role |
author |
author2 |
Jorge, Joao Atilio Souza Guimaraes, Luis Henrique |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Valera, Larissa Serrani [UNESP] Jorge, Joao Atilio Souza Guimaraes, Luis Henrique |
dc.subject.por.fl_str_mv |
Aspergillus Microbial enzymes Solid-state fermentation Tannase Tannic acid |
topic |
Aspergillus Microbial enzymes Solid-state fermentation Tannase Tannic acid |
description |
Background: Tannases are enzymes with biotechnological potential produced mainly by microorganisms as filamentous fungi. In this context, the production and characterization of a multi-tolerant tannase from Aspergillus carbonarius is described. Results: The filamentous fungus A. carbonarius produced high levels of tannase when cultivated under solid-state fermentation using green tea leaves as substrate/carbon source and tapwater at a 1:1 ratio as the moisture agent for 72 h at 30 degrees C. Two tannase activity peakswere obtained during the purification step using DEAE-Cellulose. The second peak (peak II) was purified 11-fold with 14% recovery from a Sepharose CL-6B chromatographic column. The tannase from peak II (tannase II) was characterized as a heterodimeric glycoprotein of 134.89 kDa, estimated through gel filtration, with subunits of 65 kDa and 100 kDa, estimated through SDS-PAGE, and 48% carbohydrate content. The optimal temperature and pH for tannase II activity was 60 degrees C and 5.0, respectively. The enzyme was fully stable at temperatures ranging from 20-60 degrees C for 120 min, and the half-life (T1/2) at 75 degrees C was 62 min. The activation energy was 28.93 kJ/mol. After incubation at pH 5.0 for 60 min, 75% of the enzyme activity was maintained. However, enzyme activity was increased in the presence of AgNO3 and it was tolerant to solvents and detergents. Tannase II exhibited a better affinity for methyl gallate (Km = 1.42 mM) rather than for tannic acid (Km = 2.2 mM). Conclusion: A. carbonarius tannase presented interesting properties as, for example, multi-tolerance, which highlight its potential for future application. (C) 2015 Pontificia Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. All rights reserved. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-11-01 2018-11-26T15:28:14Z 2018-11-26T15:28:14Z |
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/10.1016/j.ejbt.2015.09.008 Electronic Journal Of Biotechnology. Valparaiso: Univ Catolica De Valparaiso, v. 18, n. 6, p. 464-470, 2015. 0717-3458 http://hdl.handle.net/11449/158592 10.1016/j.ejbt.2015.09.008 WOS:000365070500013 WOS000365070500013.pdf |
url |
http://dx.doi.org/10.1016/j.ejbt.2015.09.008 http://hdl.handle.net/11449/158592 |
identifier_str_mv |
Electronic Journal Of Biotechnology. Valparaiso: Univ Catolica De Valparaiso, v. 18, n. 6, p. 464-470, 2015. 0717-3458 10.1016/j.ejbt.2015.09.008 WOS:000365070500013 WOS000365070500013.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Electronic Journal Of Biotechnology 0,537 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
464-470 application/pdf |
dc.publisher.none.fl_str_mv |
Univ Catolica De Valparaiso |
publisher.none.fl_str_mv |
Univ Catolica De Valparaiso |
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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1808128488613347328 |