Xylanase production by Aspergillus awamori under solid state fermentation conditions on tomato pomace
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , |
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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Repositório Institucional da UNESP |
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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 |
|
_version_ |
1808128930532556800 |