Production and action pattern of inulinase from Aspergillus Niger-245: hydrolysis of inulin from several sources
Autor(a) principal: | |
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Data de Publicação: | 1998 |
Outros Autores: | , , |
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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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 DArcadiaBelote,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 DArcadia 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 DArcadia |
author_facet |
Cruz,Vinícius DArcadia 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 DArcadia 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 |
format |
article |
status_str |
publishedVersion |
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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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 |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Revista de Microbiologia |
collection |
Revista de Microbiologia |
repository.name.fl_str_mv |
Revista de Microbiologia - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||revmicro@icb.usp.br |
_version_ |
1754821030162989056 |