Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase
Autor(a) principal: | |
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Data de Publicação: | 2003 |
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=S1516-89132003000200007 |
Resumo: | One hundred and twenty five soil samples were collected from the regions of roots of corn, cassava, potato, bean, sugar cane, soya, and pumpkin. From these, 75 strains were isolated that produced a yellowish halo surrounding the colonies, due to a phenolphtalein-cyclodextrin (CD) complex, and these were selected as alkalophilic CGTase-producing bacteria. All the 75 strains were identified as Bacillus firmus by microscopy and biochemical tests. The activity of the CGTase's varied from 2² to 2(10) dilutions,when assayed by CD-trichloroethylene (TCE)-complex precipitation. Strain 31 that produced the enzyme at the higher level was selected, and its enzyme was partially purified by starch adsorption (x 17) in a yield of 51%. Maximum enzyme activity occurred at pH 5.5 and 8.5. At pH 5.5, the optimum temperature was 60°C. On increased from 30°C to 85°C, the thermodynamic parameter for activation energy was 8.27 kcal.mol-1. The enzyme was inhibited by Ca2+, Mg2+, Fe2+, Cu2+, Mn2+, and Zn2+. |
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Brazilian Archives of Biology and Technology |
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Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferaseCyclodextrin glycosyltransferaseBacillus firmuscharacterizationOne hundred and twenty five soil samples were collected from the regions of roots of corn, cassava, potato, bean, sugar cane, soya, and pumpkin. From these, 75 strains were isolated that produced a yellowish halo surrounding the colonies, due to a phenolphtalein-cyclodextrin (CD) complex, and these were selected as alkalophilic CGTase-producing bacteria. All the 75 strains were identified as Bacillus firmus by microscopy and biochemical tests. The activity of the CGTase's varied from 2² to 2(10) dilutions,when assayed by CD-trichloroethylene (TCE)-complex precipitation. Strain 31 that produced the enzyme at the higher level was selected, and its enzyme was partially purified by starch adsorption (x 17) in a yield of 51%. Maximum enzyme activity occurred at pH 5.5 and 8.5. At pH 5.5, the optimum temperature was 60°C. On increased from 30°C to 85°C, the thermodynamic parameter for activation energy was 8.27 kcal.mol-1. The enzyme was inhibited by Ca2+, Mg2+, Fe2+, Cu2+, Mn2+, and Zn2+.Instituto de Tecnologia do Paraná - Tecpar2003-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132003000200007Brazilian Archives of Biology and Technology v.46 n.2 2003reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132003000200007info:eu-repo/semantics/openAccessHiguti,lma HirokoGrande,Simone WichertSacco,RobertaNascimento,Aguinaldo José doeng2003-07-29T00:00:00Zoai:scielo:S1516-89132003000200007Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2003-07-29T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
title |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
spellingShingle |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase Higuti,lma Hiroko Cyclodextrin glycosyltransferase Bacillus firmus characterization |
title_short |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
title_full |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
title_fullStr |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
title_full_unstemmed |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
title_sort |
Isolation of alkalophilic CGTase-producing bacteria and characterization of cyclodextrin-glycosyltransferase |
author |
Higuti,lma Hiroko |
author_facet |
Higuti,lma Hiroko Grande,Simone Wichert Sacco,Roberta Nascimento,Aguinaldo José do |
author_role |
author |
author2 |
Grande,Simone Wichert Sacco,Roberta Nascimento,Aguinaldo José do |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Higuti,lma Hiroko Grande,Simone Wichert Sacco,Roberta Nascimento,Aguinaldo José do |
dc.subject.por.fl_str_mv |
Cyclodextrin glycosyltransferase Bacillus firmus characterization |
topic |
Cyclodextrin glycosyltransferase Bacillus firmus characterization |
description |
One hundred and twenty five soil samples were collected from the regions of roots of corn, cassava, potato, bean, sugar cane, soya, and pumpkin. From these, 75 strains were isolated that produced a yellowish halo surrounding the colonies, due to a phenolphtalein-cyclodextrin (CD) complex, and these were selected as alkalophilic CGTase-producing bacteria. All the 75 strains were identified as Bacillus firmus by microscopy and biochemical tests. The activity of the CGTase's varied from 2² to 2(10) dilutions,when assayed by CD-trichloroethylene (TCE)-complex precipitation. Strain 31 that produced the enzyme at the higher level was selected, and its enzyme was partially purified by starch adsorption (x 17) in a yield of 51%. Maximum enzyme activity occurred at pH 5.5 and 8.5. At pH 5.5, the optimum temperature was 60°C. On increased from 30°C to 85°C, the thermodynamic parameter for activation energy was 8.27 kcal.mol-1. The enzyme was inhibited by Ca2+, Mg2+, Fe2+, Cu2+, Mn2+, and Zn2+. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-03-01 |
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=S1516-89132003000200007 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132003000200007 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132003000200007 |
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.46 n.2 2003 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_ |
1750318269155246080 |