Colorimetric determination of alpha and beta-cyclodextrins and studies on optimization of CGTase production from B. firmus using factorial designs

Detalhes bibliográficos
Autor(a) principal: Higuti,Ilma Hiroko
Data de Publicação: 2004
Outros Autores: Silva,Priscila Anunciação da, Papp,Juliana, Okiyama,Vivian Mayumi de Eiróz, Andrade,Edicléia Alves de, Marcondes,Aluizio de Abreu, Nascimento,Aguinaldo José do
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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spelling 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
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dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132004000600001
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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
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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
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