Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger

Detalhes bibliográficos
Autor(a) principal: Benedetti, Ana Cláudia Elias Pião [UNESP]
Data de Publicação: 2013
Outros Autores: da Costa, Eliana Dantas [UNESP], Aragon, Caio Casale [UNESP], dos Santos, Andréa Francisco [UNESP], Goulart, Antônio José [UNESP], Attili-Angelis, Derlene [UNESP], Monti, Rubens [UNESP]
Tipo de documento: Artigo
Idioma: eng
por
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://serv-bib.fcfar.unesp.br/seer/index.php/Cien_Farm/article/view/2335
http://hdl.handle.net/11449/75039
Resumo: A strain of the flamentous fungus Aspergillus niger was isolated and shown to possess extracellular xylanolytic activity. These enzymes have biotechnological potential and can be employed in various industries. This fungus produced its highest xylanase activity in a medium made up of 0.1% CaCO3, 0.5% NaCl, 0.1% NH4Cl, 0.5% corn steep liquor and 1% carbon source, at pH 8.0. A low-cost hemicellulose residue (powdered corncob) proved to be an excellent inducer of the A. niger xylanolytic complex. Filtration of the crude culture medium with suspended kaolin was ideal for to clarify the extract and led to partial purifcation of the xylanolytic activity. The apparent molecular mass of the xylanase was about 32.3 kDa. Maximum enzyme activity occurred at pH 5.0 and 55-60oC. Apparent Km was 10.41 ± 0.282 mg/mL and Vmax was 3.32 ± 0.053 U/mg protein, with birchwood xylan as the substrate. Activation energy was 4.55 kcal/mol and half-life of the crude enzyme at 60oC was 30 minutes. Addition of 2% glucose to the culture medium supplemented with xylan repressed xylanase production, but in the presence of xylose the enzyme production was not affected.
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spelling Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus nigerLow-cost carbon sources for the production of a thermostable xylanase by Aspergillus nigerAgroindustrial residuesAspergillus nigerThermostabilityXylanolytic enzymesbagassekaolinunclassified drugxylanxylan 1, 4 beta xylosidasexylan endo 1, 3 beta xylosidaseanimal cellAspergillus versicolorcarbon sourcechromatographyenzyme synthesisfungal cell culturehydrolysis kineticskineticsnonhumanpHpolyacrylamide gel electrophoresisprotein contentprotein determinationtemperaturethin layer chromatographywheat branA strain of the flamentous fungus Aspergillus niger was isolated and shown to possess extracellular xylanolytic activity. These enzymes have biotechnological potential and can be employed in various industries. This fungus produced its highest xylanase activity in a medium made up of 0.1% CaCO3, 0.5% NaCl, 0.1% NH4Cl, 0.5% corn steep liquor and 1% carbon source, at pH 8.0. A low-cost hemicellulose residue (powdered corncob) proved to be an excellent inducer of the A. niger xylanolytic complex. Filtration of the crude culture medium with suspended kaolin was ideal for to clarify the extract and led to partial purifcation of the xylanolytic activity. The apparent molecular mass of the xylanase was about 32.3 kDa. Maximum enzyme activity occurred at pH 5.0 and 55-60oC. Apparent Km was 10.41 ± 0.282 mg/mL and Vmax was 3.32 ± 0.053 U/mg protein, with birchwood xylan as the substrate. Activation energy was 4.55 kcal/mol and half-life of the crude enzyme at 60oC was 30 minutes. Addition of 2% glucose to the culture medium supplemented with xylan repressed xylanase production, but in the presence of xylose the enzyme production was not affected.Fontes de carbono de baixo custo para a produção de xilanase termoestável por Aspergillus niger Uma linhagem do fungo filamentoso Aspergillus niger foi isolada e apresentou atividade xilanolítica extracelular. Estas enzimas possuem grande potencial biotecnológico e podem ser aplicadas em diversas indústrias. O fungo produziu sua maior atividade de xilanase em um meio contendo CaCO 3 0,1%, NaCl 0,5%, NH 4 Cl 0,1%, 0,5% água de maceração de milho e 1% de fonte de carbono, em pH 8,0. Um resíduo lignocelulósico de baixo custo (sabugo de milho em pó) mostrou ser um excelente indutor do complexo xilanolítico em A. niger . A filtração do extrato cru com caulim foi ideal para a clarificação do extrato e levou à purificação parcial da enzima. A massa molecular aparente da xilanase foi de 32,3 kDa. A máxima atividade da enzima ocorreu em pH 5,0 e a 55-60ºC. O K m aparente foi de 10,41 ± 0,282 mg/mL e a V max foi de 3,32 ± 0,053 U/mg proteína, utilizando-se xilana birchwood como substrato. A energia de ativação foi de 4,55 kcal/mol, e a meia-vida da enzima a 60ºC foi de 30 minutos. A adição de 2% de glicose ao meio de cultura suplementado com xilana reprimiu a produção de xilanase, mas em presença de xilose a produção da enzima não foi afetada.Universidade Estadual Paulista (UNESP) Department of Food and Nutrition, Araraquara, SPUniversidade Estadual Paulista (UNESP) Department of Biochemistry and Chemical Technology Institute of Chemistry, Araraquara, SPUniversidade Estadual Paulista (UNESP) Center of Studies of Social Insects Institute of Biosciences, Rio Claro, SPUniversidade Estadual Paulista (UNESP) Department of Food and Nutrition, Araraquara, SPUniversidade Estadual Paulista (UNESP) Department of Biochemistry and Chemical Technology Institute of Chemistry, Araraquara, SPUniversidade Estadual Paulista (UNESP) Center of Studies of Social Insects Institute of Biosciences, Rio Claro, SPUniversidade Estadual Paulista (Unesp)Benedetti, Ana Cláudia Elias Pião [UNESP]da Costa, Eliana Dantas [UNESP]Aragon, Caio Casale [UNESP]dos Santos, Andréa Francisco [UNESP]Goulart, Antônio José [UNESP]Attili-Angelis, Derlene [UNESP]Monti, Rubens [UNESP]2014-05-27T11:28:49Z2014-05-27T11:28:49Z2013-04-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article25-31application/pdfhttp://serv-bib.fcfar.unesp.br/seer/index.php/Cien_Farm/article/view/2335Revista de Ciencias Farmaceuticas Basica e Aplicada, v. 34, n. 1, p. 25-31, 2013.1808-4532http://hdl.handle.net/11449/750392-s2.0-848760155932-s2.0-84876015593.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengporRevista de Ciências Farmacêuticas Básica e Aplicada0,131info:eu-repo/semantics/openAccess2024-06-21T12:46:32Zoai:repositorio.unesp.br:11449/75039Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T14:02:49.594579Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
Low-cost carbon sources for the production of a thermostable xylanase by Aspergillus niger
title Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
spellingShingle Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
Benedetti, Ana Cláudia Elias Pião [UNESP]
Agroindustrial residues
Aspergillus niger
Thermostability
Xylanolytic enzymes
bagasse
kaolin
unclassified drug
xylan
xylan 1, 4 beta xylosidase
xylan endo 1, 3 beta xylosidase
animal cell
Aspergillus versicolor
carbon source
chromatography
enzyme synthesis
fungal cell culture
hydrolysis kinetics
kinetics
nonhuman
pH
polyacrylamide gel electrophoresis
protein content
protein determination
temperature
thin layer chromatography
wheat bran
title_short Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
title_full Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
title_fullStr Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
title_full_unstemmed Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
title_sort Fontes de carbono de baixo custo para a produção de xilanase termoestável por aspergillus niger
author Benedetti, Ana Cláudia Elias Pião [UNESP]
author_facet Benedetti, Ana Cláudia Elias Pião [UNESP]
da Costa, Eliana Dantas [UNESP]
Aragon, Caio Casale [UNESP]
dos Santos, Andréa Francisco [UNESP]
Goulart, Antônio José [UNESP]
Attili-Angelis, Derlene [UNESP]
Monti, Rubens [UNESP]
author_role author
author2 da Costa, Eliana Dantas [UNESP]
Aragon, Caio Casale [UNESP]
dos Santos, Andréa Francisco [UNESP]
Goulart, Antônio José [UNESP]
Attili-Angelis, Derlene [UNESP]
Monti, Rubens [UNESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Benedetti, Ana Cláudia Elias Pião [UNESP]
da Costa, Eliana Dantas [UNESP]
Aragon, Caio Casale [UNESP]
dos Santos, Andréa Francisco [UNESP]
Goulart, Antônio José [UNESP]
Attili-Angelis, Derlene [UNESP]
Monti, Rubens [UNESP]
dc.subject.por.fl_str_mv Agroindustrial residues
Aspergillus niger
Thermostability
Xylanolytic enzymes
bagasse
kaolin
unclassified drug
xylan
xylan 1, 4 beta xylosidase
xylan endo 1, 3 beta xylosidase
animal cell
Aspergillus versicolor
carbon source
chromatography
enzyme synthesis
fungal cell culture
hydrolysis kinetics
kinetics
nonhuman
pH
polyacrylamide gel electrophoresis
protein content
protein determination
temperature
thin layer chromatography
wheat bran
topic Agroindustrial residues
Aspergillus niger
Thermostability
Xylanolytic enzymes
bagasse
kaolin
unclassified drug
xylan
xylan 1, 4 beta xylosidase
xylan endo 1, 3 beta xylosidase
animal cell
Aspergillus versicolor
carbon source
chromatography
enzyme synthesis
fungal cell culture
hydrolysis kinetics
kinetics
nonhuman
pH
polyacrylamide gel electrophoresis
protein content
protein determination
temperature
thin layer chromatography
wheat bran
description A strain of the flamentous fungus Aspergillus niger was isolated and shown to possess extracellular xylanolytic activity. These enzymes have biotechnological potential and can be employed in various industries. This fungus produced its highest xylanase activity in a medium made up of 0.1% CaCO3, 0.5% NaCl, 0.1% NH4Cl, 0.5% corn steep liquor and 1% carbon source, at pH 8.0. A low-cost hemicellulose residue (powdered corncob) proved to be an excellent inducer of the A. niger xylanolytic complex. Filtration of the crude culture medium with suspended kaolin was ideal for to clarify the extract and led to partial purifcation of the xylanolytic activity. The apparent molecular mass of the xylanase was about 32.3 kDa. Maximum enzyme activity occurred at pH 5.0 and 55-60oC. Apparent Km was 10.41 ± 0.282 mg/mL and Vmax was 3.32 ± 0.053 U/mg protein, with birchwood xylan as the substrate. Activation energy was 4.55 kcal/mol and half-life of the crude enzyme at 60oC was 30 minutes. Addition of 2% glucose to the culture medium supplemented with xylan repressed xylanase production, but in the presence of xylose the enzyme production was not affected.
publishDate 2013
dc.date.none.fl_str_mv 2013-04-01
2014-05-27T11:28:49Z
2014-05-27T11:28:49Z
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://serv-bib.fcfar.unesp.br/seer/index.php/Cien_Farm/article/view/2335
Revista de Ciencias Farmaceuticas Basica e Aplicada, v. 34, n. 1, p. 25-31, 2013.
1808-4532
http://hdl.handle.net/11449/75039
2-s2.0-84876015593
2-s2.0-84876015593.pdf
url http://serv-bib.fcfar.unesp.br/seer/index.php/Cien_Farm/article/view/2335
http://hdl.handle.net/11449/75039
identifier_str_mv Revista de Ciencias Farmaceuticas Basica e Aplicada, v. 34, n. 1, p. 25-31, 2013.
1808-4532
2-s2.0-84876015593
2-s2.0-84876015593.pdf
dc.language.iso.fl_str_mv eng
por
language eng
por
dc.relation.none.fl_str_mv Revista de Ciências Farmacêuticas Básica e Aplicada
0,131
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 25-31
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
_version_ 1808128308264566784

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