Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132004000600001 |
Resumo: | Cyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) production from B. firmus, isolated from soil of Curitiba, PR, was optimized in shake flask using an experimental design approach. The CGTase was produced when the carbon source was starch and beta-CD, but when simple sugars such as glucose, galactose, lactose, sucrose, and maltose were used, there was no enzyme production. CGTase production was the same with either organic nitrogen or inorganic nitrogen source. CGTase activity decreased 2-fold when incubation temperature was increased from 28 to 37 ° C, and decreased 2.1- fold when the initial pH was lowered from 10.3 to 7.4. The colorimetric determinations of alpha - and beta -CD were analyzed as a non-linear relationship and the equilibrium constant for alpha -CD/methyl orange and beta -CD/phenolphthalein complexes were 7.69 x 10³ L / mol and 2.33 x 10³ L/ mol, respectively. |
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Brazilian Archives of Biology and Technology |
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Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designsCyclodextrin glycosyltransferaseBacillus firmuscyclodextrinsCyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) production from B. firmus, isolated from soil of Curitiba, PR, was optimized in shake flask using an experimental design approach. The CGTase was produced when the carbon source was starch and beta-CD, but when simple sugars such as glucose, galactose, lactose, sucrose, and maltose were used, there was no enzyme production. CGTase production was the same with either organic nitrogen or inorganic nitrogen source. CGTase activity decreased 2-fold when incubation temperature was increased from 28 to 37 ° C, and decreased 2.1- fold when the initial pH was lowered from 10.3 to 7.4. The colorimetric determinations of alpha - and beta -CD were analyzed as a non-linear relationship and the equilibrium constant for alpha -CD/methyl orange and beta -CD/phenolphthalein complexes were 7.69 x 10³ L / mol and 2.33 x 10³ L/ mol, respectively.Instituto de Tecnologia do Paraná - Tecpar2004-11-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132004000600001Brazilian Archives of Biology and Technology v.47 n.6 2004reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132004000600001info:eu-repo/semantics/openAccessHiguti,Ilma HirokoSilva,Priscila Anunciação daPapp,JulianaOkiyama,Vivian Mayumi de EirózAndrade,Edicléia Alves deMarcondes,Aluizio de AbreuNascimento,Aguinaldo José doeng2005-02-04T00:00:00Zoai:scielo:S1516-89132004000600001Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2005-02-04T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
title |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
spellingShingle |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs Higuti,Ilma Hiroko Cyclodextrin glycosyltransferase Bacillus firmus cyclodextrins |
title_short |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
title_full |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
title_fullStr |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
title_full_unstemmed |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
title_sort |
Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs |
author |
Higuti,Ilma Hiroko |
author_facet |
Higuti,Ilma Hiroko Silva,Priscila Anunciação da Papp,Juliana Okiyama,Vivian Mayumi de Eiróz Andrade,Edicléia Alves de Marcondes,Aluizio de Abreu Nascimento,Aguinaldo José do |
author_role |
author |
author2 |
Silva,Priscila Anunciação da Papp,Juliana Okiyama,Vivian Mayumi de Eiróz Andrade,Edicléia Alves de Marcondes,Aluizio de Abreu Nascimento,Aguinaldo José do |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Higuti,Ilma Hiroko Silva,Priscila Anunciação da Papp,Juliana Okiyama,Vivian Mayumi de Eiróz Andrade,Edicléia Alves de Marcondes,Aluizio de Abreu Nascimento,Aguinaldo José do |
dc.subject.por.fl_str_mv |
Cyclodextrin glycosyltransferase Bacillus firmus cyclodextrins |
topic |
Cyclodextrin glycosyltransferase Bacillus firmus cyclodextrins |
description |
Cyclodextrin glycosyltransferase (EC 2.4.1.19, CGTase) production from B. firmus, isolated from soil of Curitiba, PR, was optimized in shake flask using an experimental design approach. The CGTase was produced when the carbon source was starch and beta-CD, but when simple sugars such as glucose, galactose, lactose, sucrose, and maltose were used, there was no enzyme production. CGTase production was the same with either organic nitrogen or inorganic nitrogen source. CGTase activity decreased 2-fold when incubation temperature was increased from 28 to 37 ° C, and decreased 2.1- fold when the initial pH was lowered from 10.3 to 7.4. The colorimetric determinations of alpha - and beta -CD were analyzed as a non-linear relationship and the equilibrium constant for alpha -CD/methyl orange and beta -CD/phenolphthalein complexes were 7.69 x 10³ L / mol and 2.33 x 10³ L/ mol, respectively. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-11-01 |
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=S1516-89132004000600001 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132004000600001 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132004000600001 |
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 |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.47 n.6 2004 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318269920706560 |