Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources

Detalhes bibliográficos
Autor(a) principal: Cruz,Vinícius D’Arcadia
Data de Publicação: 1998
Outros Autores: Belote,Juliana Gisele, Belline,Márcia Zilioli, Cruz,Rubens
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Revista de Microbiologia
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000400013
Resumo: A strain of Aspergillus niger isolated from soil samples showed great capacity to produce extracellular inulinase. Although the enzyme has been synthesized in presence of monosaccharides, sucrose and sugar cane molasse, the productivity was significantly higher (p<0.05) when the microorganism was inoculated in media formulated with dahlia extract and pure inulin, as carbon sources. With regard to the nitrogen source, the best results were obtained with casein and other sources of proteic nitrogen, comparatively to the mineral nitrogen. However, statistic significance (p<0.01) only was found between the productivity obtained in the medium prepared with casein and ammonium sulphate. The optimum pH of the purified enzyme for inulin hydrolysis was found between 4.0 and 4.5 and the optimun temperature at 60oC. When treated by 30 minutes in this temperature no loss of activity was observed. The enzyme showed capacity to hydrolyse sucrose, raffinose and inulin from which it liberated only fructose units showing, therefore, an exo-action mechanism. Acting on inulins from several sources, the enzyme showed larger hydrolysis speed on the polissaccharide from chicory (Cichorium intibus), comparatively, to the inulins from dahlia (Dahlia pinnata) and Jerusalem artichoke (Helianthus tuberosus) roots.
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spelling Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sourcesinulinaseAspergillus nigerfructose syrupinulinA strain of Aspergillus niger isolated from soil samples showed great capacity to produce extracellular inulinase. Although the enzyme has been synthesized in presence of monosaccharides, sucrose and sugar cane molasse, the productivity was significantly higher (p<0.05) when the microorganism was inoculated in media formulated with dahlia extract and pure inulin, as carbon sources. With regard to the nitrogen source, the best results were obtained with casein and other sources of proteic nitrogen, comparatively to the mineral nitrogen. However, statistic significance (p<0.01) only was found between the productivity obtained in the medium prepared with casein and ammonium sulphate. The optimum pH of the purified enzyme for inulin hydrolysis was found between 4.0 and 4.5 and the optimun temperature at 60oC. When treated by 30 minutes in this temperature no loss of activity was observed. The enzyme showed capacity to hydrolyse sucrose, raffinose and inulin from which it liberated only fructose units showing, therefore, an exo-action mechanism. Acting on inulins from several sources, the enzyme showed larger hydrolysis speed on the polissaccharide from chicory (Cichorium intibus), comparatively, to the inulins from dahlia (Dahlia pinnata) and Jerusalem artichoke (Helianthus tuberosus) roots.Sociedade Brasileira de Microbiologia1998-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000400013Revista de Microbiologia v.29 n.4 1998reponame:Revista de Microbiologiainstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S0001-37141998000400013info:eu-repo/semantics/openAccessCruz,Vinícius D’ArcadiaBelote,Juliana GiseleBelline,Márcia ZilioliCruz,Rubenseng1999-05-27T00:00:00Zoai:scielo:S0001-37141998000400013Revistahttps://www.scielo.br/j/rm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||revmicro@icb.usp.br0001-37140001-3714opendoar:1999-05-27T00:00Revista de Microbiologia - Sociedade Brasileira de Microbiologia (SBM)false
dc.title.none.fl_str_mv Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
title Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
spellingShingle Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
Cruz,Vinícius D’Arcadia
inulinase
Aspergillus niger
fructose syrup
inulin
title_short Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
title_full Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
title_fullStr Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
title_full_unstemmed Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
title_sort Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
author Cruz,Vinícius D’Arcadia
author_facet Cruz,Vinícius D’Arcadia
Belote,Juliana Gisele
Belline,Márcia Zilioli
Cruz,Rubens
author_role author
author2 Belote,Juliana Gisele
Belline,Márcia Zilioli
Cruz,Rubens
author2_role author
author
author
dc.contributor.author.fl_str_mv Cruz,Vinícius D’Arcadia
Belote,Juliana Gisele
Belline,Márcia Zilioli
Cruz,Rubens
dc.subject.por.fl_str_mv inulinase
Aspergillus niger
fructose syrup
inulin
topic inulinase
Aspergillus niger
fructose syrup
inulin
description A strain of Aspergillus niger isolated from soil samples showed great capacity to produce extracellular inulinase. Although the enzyme has been synthesized in presence of monosaccharides, sucrose and sugar cane molasse, the productivity was significantly higher (p<0.05) when the microorganism was inoculated in media formulated with dahlia extract and pure inulin, as carbon sources. With regard to the nitrogen source, the best results were obtained with casein and other sources of proteic nitrogen, comparatively to the mineral nitrogen. However, statistic significance (p<0.01) only was found between the productivity obtained in the medium prepared with casein and ammonium sulphate. The optimum pH of the purified enzyme for inulin hydrolysis was found between 4.0 and 4.5 and the optimun temperature at 60oC. When treated by 30 minutes in this temperature no loss of activity was observed. The enzyme showed capacity to hydrolyse sucrose, raffinose and inulin from which it liberated only fructose units showing, therefore, an exo-action mechanism. Acting on inulins from several sources, the enzyme showed larger hydrolysis speed on the polissaccharide from chicory (Cichorium intibus), comparatively, to the inulins from dahlia (Dahlia pinnata) and Jerusalem artichoke (Helianthus tuberosus) roots.
publishDate 1998
dc.date.none.fl_str_mv 1998-10-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000400013
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141998000400013
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0001-37141998000400013
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dc.format.none.fl_str_mv text/html
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 Revista de Microbiologia v.29 n.4 1998
reponame:Revista de Microbiologia
instname:Sociedade Brasileira de Microbiologia (SBM)
instacron:SBM
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collection Revista de Microbiologia
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