Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources

Detalhes bibliográficos
Autor(a) principal: Pavezzi,Fabiana Carina
Data de Publicação: 2008
Outros Autores: Gomes,Eleni, Silva,Roberto da
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Microbiology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000100024
Resumo: Glucoamylase is widely used in the food industry to produce high glucose syrup, and also in fermentation processes for production beer and ethanol. In this work the productivity of the glucoamylase of Aspergillus awamori expressed by the yeast Saccharomyces cerevisiae, produced in submerged fermentation using different starches, was evaluated and characterized physico-chemically. The enzyme presented high specific activity, 13.8 U/mgprotein or 2.9 U/mgbiomass, after 48 h of fermentation using soluble starch as substrate. Glucoamylase presented optimum activity at temperature of 55ºC, and, in the substratum absence, the thermostability was for 1h at 50ºC. The optimum pH of activity was pH 3.5 - 4.0 and the pH stability between 5.0 and 7.0. The half life at 65ºC was at 30.2 min, and the thermal energy of denaturation was 234.3 KJ mol-1. The hydrolysis of different substrate showed the enzyme's preference for the substrate with a larger polymerization degree. The gelatinized corn starch was the substratum most susceptible to the enzymatic action.
id SBM-1_a427f4615c6c8b50940c9e9485a3e76a
oai_identifier_str oai:scielo:S1517-83822008000100024
network_acronym_str SBM-1
network_name_str Brazilian Journal of Microbiology
repository_id_str
spelling Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sourcesGlucoamylaseAspergillus awamoriSaccharomyces cerevisiaeCorn starchPotato starchCassava starchGlucoamylase is widely used in the food industry to produce high glucose syrup, and also in fermentation processes for production beer and ethanol. In this work the productivity of the glucoamylase of Aspergillus awamori expressed by the yeast Saccharomyces cerevisiae, produced in submerged fermentation using different starches, was evaluated and characterized physico-chemically. The enzyme presented high specific activity, 13.8 U/mgprotein or 2.9 U/mgbiomass, after 48 h of fermentation using soluble starch as substrate. Glucoamylase presented optimum activity at temperature of 55ºC, and, in the substratum absence, the thermostability was for 1h at 50ºC. The optimum pH of activity was pH 3.5 - 4.0 and the pH stability between 5.0 and 7.0. The half life at 65ºC was at 30.2 min, and the thermal energy of denaturation was 234.3 KJ mol-1. The hydrolysis of different substrate showed the enzyme's preference for the substrate with a larger polymerization degree. The gelatinized corn starch was the substratum most susceptible to the enzymatic action.Sociedade Brasileira de Microbiologia2008-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000100024Brazilian Journal of Microbiology v.39 n.1 2008reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822008000100024info:eu-repo/semantics/openAccessPavezzi,Fabiana CarinaGomes,EleniSilva,Roberto daeng2008-04-11T00:00:00Zoai:scielo:S1517-83822008000100024Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2008-04-11T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false
dc.title.none.fl_str_mv Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
title Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
spellingShingle Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
Pavezzi,Fabiana Carina
Glucoamylase
Aspergillus awamori
Saccharomyces cerevisiae
Corn starch
Potato starch
Cassava starch
title_short Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
title_full Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
title_fullStr Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
title_full_unstemmed Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
title_sort Production and characterization of glucoamylase from fungus Aspergillus awamori expressed in yeast Saccharomyces cerevisiae using different carbon sources
author Pavezzi,Fabiana Carina
author_facet Pavezzi,Fabiana Carina
Gomes,Eleni
Silva,Roberto da
author_role author
author2 Gomes,Eleni
Silva,Roberto da
author2_role author
author
dc.contributor.author.fl_str_mv Pavezzi,Fabiana Carina
Gomes,Eleni
Silva,Roberto da
dc.subject.por.fl_str_mv Glucoamylase
Aspergillus awamori
Saccharomyces cerevisiae
Corn starch
Potato starch
Cassava starch
topic Glucoamylase
Aspergillus awamori
Saccharomyces cerevisiae
Corn starch
Potato starch
Cassava starch
description Glucoamylase is widely used in the food industry to produce high glucose syrup, and also in fermentation processes for production beer and ethanol. In this work the productivity of the glucoamylase of Aspergillus awamori expressed by the yeast Saccharomyces cerevisiae, produced in submerged fermentation using different starches, was evaluated and characterized physico-chemically. The enzyme presented high specific activity, 13.8 U/mgprotein or 2.9 U/mgbiomass, after 48 h of fermentation using soluble starch as substrate. Glucoamylase presented optimum activity at temperature of 55ºC, and, in the substratum absence, the thermostability was for 1h at 50ºC. The optimum pH of activity was pH 3.5 - 4.0 and the pH stability between 5.0 and 7.0. The half life at 65ºC was at 30.2 min, and the thermal energy of denaturation was 234.3 KJ mol-1. The hydrolysis of different substrate showed the enzyme's preference for the substrate with a larger polymerization degree. The gelatinized corn starch was the substratum most susceptible to the enzymatic action.
publishDate 2008
dc.date.none.fl_str_mv 2008-03-01
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=S1517-83822008000100024
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822008000100024
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1517-83822008000100024
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 Brazilian Journal of Microbiology v.39 n.1 2008
reponame:Brazilian Journal of Microbiology
instname:Sociedade Brasileira de Microbiologia (SBM)
instacron:SBM
instname_str Sociedade Brasileira de Microbiologia (SBM)
instacron_str SBM
institution SBM
reponame_str Brazilian Journal of Microbiology
collection Brazilian Journal of Microbiology
repository.name.fl_str_mv Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)
repository.mail.fl_str_mv bjm@sbmicrobiologia.org.br||mbmartin@usp.br
_version_ 1752122201475121152