Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace

Detalhes bibliográficos
Autor(a) principal: Umsza-Guez, Marcelo A. [UNESP]
Data de Publicação: 2011
Outros Autores: Díaz, Ana B., Ory, Ignacio de, Blandino, Ana, Gomes, Eleni [UNESP], Caro, Ildefonso
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1590/S1517-83822011000400046
http://hdl.handle.net/11449/22189
Resumo: In this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and α-amylase. The principal step of the process is the solid state fermentation (SSF) of this residue by Aspergillus awamori. In several laboratory experiments, maximum xylanase and exo-PG activities were measured during the first days of culture, reaching values around 100 and 80 IU/gds (international units of enzyme activity per gram of dried solid), respectively. For CMCase and α-amylase production remained almost constant along fermentation, with average values of 19 and 21.5 IU/gds, respectively. Experiments carried out in a plate-type bioreactor at lab scale showed a clear positive effect of aeration on xylanase and CMCase, while the opposite was observed for exo-PG and α-amylase. In general, xylanase was the enzyme produced in higher levels, thus the optimum conditions for the determination of the enzyme activity was characterized. The xylanase activity shows an optimum pH of 5 and an optimum temperature of 50 ºC. The enzyme is activated by Mg2+, but strongly inhibited by Hg2+ and Cu2+. The enzymatic activity remains quite high if the extract is preserved in a range of pH from 3 to 10 and a temperature between 30 ºC to 40 ºC.
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spelling Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomaceSolid state fermentation (SSF)tomato pomacehydrolytic enzymesplate-type bioreactorxylanase productionIn this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and α-amylase. The principal step of the process is the solid state fermentation (SSF) of this residue by Aspergillus awamori. In several laboratory experiments, maximum xylanase and exo-PG activities were measured during the first days of culture, reaching values around 100 and 80 IU/gds (international units of enzyme activity per gram of dried solid), respectively. For CMCase and α-amylase production remained almost constant along fermentation, with average values of 19 and 21.5 IU/gds, respectively. Experiments carried out in a plate-type bioreactor at lab scale showed a clear positive effect of aeration on xylanase and CMCase, while the opposite was observed for exo-PG and α-amylase. In general, xylanase was the enzyme produced in higher levels, thus the optimum conditions for the determination of the enzyme activity was characterized. The xylanase activity shows an optimum pH of 5 and an optimum temperature of 50 ºC. The enzyme is activated by Mg2+, but strongly inhibited by Hg2+ and Cu2+. The enzymatic activity remains quite high if the extract is preserved in a range of pH from 3 to 10 and a temperature between 30 ºC to 40 ºC.Ministerio de Ciência y Tecnologia of SpainFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Universidade Estadual Paulista Instituto de Biociências, Letras e Ciências Exatas Laboratório de Bioquímica e Microbiologia AplicadaUniversidad de Cádiz Facultad de Ciencias Departamento de Ingeniería Química y Tecnología de AlimentosUniversidade Estadual Paulista Instituto de Biociências, Letras e Ciências Exatas Laboratório de Bioquímica e Microbiologia AplicadaMinisterio de Ciência y Tecnologia of Spain: CTQ2006-04257/PPQSociedade Brasileira de MicrobiologiaUniversidade Estadual Paulista (Unesp)Universidad de Cádiz Facultad de Ciencias Departamento de Ingeniería Química y Tecnología de AlimentosUmsza-Guez, Marcelo A. [UNESP]Díaz, Ana B.Ory, Ignacio deBlandino, AnaGomes, Eleni [UNESP]Caro, Ildefonso2014-05-20T14:02:59Z2014-05-20T14:02:59Z2011-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1585-1597application/pdfhttp://dx.doi.org/10.1590/S1517-83822011000400046Brazilian Journal of Microbiology. Sociedade Brasileira de Microbiologia, v. 42, n. 4, p. 1585-1597, 2011.1517-8382http://hdl.handle.net/11449/2218910.1590/S1517-83822011000400046S1517-83822011000400046WOS:000300430600046S1517-83822011000400046.pdf7091241742851920SciELOreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBrazilian Journal of Microbiology1.8100,630info:eu-repo/semantics/openAccess2023-11-22T06:14:35Zoai:repositorio.unesp.br:11449/22189Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:25:30.869840Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
title Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
spellingShingle Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
Umsza-Guez, Marcelo A. [UNESP]
Solid state fermentation (SSF)
tomato pomace
hydrolytic enzymes
plate-type bioreactor
xylanase production
title_short Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
title_full Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
title_fullStr Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
title_full_unstemmed Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
title_sort Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
author Umsza-Guez, Marcelo A. [UNESP]
author_facet Umsza-Guez, Marcelo A. [UNESP]
Díaz, Ana B.
Ory, Ignacio de
Blandino, Ana
Gomes, Eleni [UNESP]
Caro, Ildefonso
author_role author
author2 Díaz, Ana B.
Ory, Ignacio de
Blandino, Ana
Gomes, Eleni [UNESP]
Caro, Ildefonso
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidad de Cádiz Facultad de Ciencias Departamento de Ingeniería Química y Tecnología de Alimentos
dc.contributor.author.fl_str_mv Umsza-Guez, Marcelo A. [UNESP]
Díaz, Ana B.
Ory, Ignacio de
Blandino, Ana
Gomes, Eleni [UNESP]
Caro, Ildefonso
dc.subject.por.fl_str_mv Solid state fermentation (SSF)
tomato pomace
hydrolytic enzymes
plate-type bioreactor
xylanase production
topic Solid state fermentation (SSF)
tomato pomace
hydrolytic enzymes
plate-type bioreactor
xylanase production
description In this work, tomato pomace, a waste abundantly available in the Mediterranean and other temperate climates agro-food industries, has been used as raw material for the production of some hydrolytic enzymes, including xylanase, exo-polygalacturonase (exo-PG), cellulase (CMCase) and α-amylase. The principal step of the process is the solid state fermentation (SSF) of this residue by Aspergillus awamori. In several laboratory experiments, maximum xylanase and exo-PG activities were measured during the first days of culture, reaching values around 100 and 80 IU/gds (international units of enzyme activity per gram of dried solid), respectively. For CMCase and α-amylase production remained almost constant along fermentation, with average values of 19 and 21.5 IU/gds, respectively. Experiments carried out in a plate-type bioreactor at lab scale showed a clear positive effect of aeration on xylanase and CMCase, while the opposite was observed for exo-PG and α-amylase. In general, xylanase was the enzyme produced in higher levels, thus the optimum conditions for the determination of the enzyme activity was characterized. The xylanase activity shows an optimum pH of 5 and an optimum temperature of 50 ºC. The enzyme is activated by Mg2+, but strongly inhibited by Hg2+ and Cu2+. The enzymatic activity remains quite high if the extract is preserved in a range of pH from 3 to 10 and a temperature between 30 ºC to 40 ºC.
publishDate 2011
dc.date.none.fl_str_mv 2011-12-01
2014-05-20T14:02:59Z
2014-05-20T14:02:59Z
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/10.1590/S1517-83822011000400046
Brazilian Journal of Microbiology. Sociedade Brasileira de Microbiologia, v. 42, n. 4, p. 1585-1597, 2011.
1517-8382
http://hdl.handle.net/11449/22189
10.1590/S1517-83822011000400046
S1517-83822011000400046
WOS:000300430600046
S1517-83822011000400046.pdf
7091241742851920
url http://dx.doi.org/10.1590/S1517-83822011000400046
http://hdl.handle.net/11449/22189
identifier_str_mv Brazilian Journal of Microbiology. Sociedade Brasileira de Microbiologia, v. 42, n. 4, p. 1585-1597, 2011.
1517-8382
10.1590/S1517-83822011000400046
S1517-83822011000400046
WOS:000300430600046
S1517-83822011000400046.pdf
7091241742851920
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Brazilian Journal of Microbiology
1.810
0,630
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1585-1597
application/pdf
dc.publisher.none.fl_str_mv Sociedade Brasileira de Microbiologia
publisher.none.fl_str_mv Sociedade Brasileira de Microbiologia
dc.source.none.fl_str_mv SciELO
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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