Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties

Detalhes bibliográficos
Autor(a) principal: Bonilha,Paulo Roberto Martins
Data de Publicação: 2006
Outros Autores: Menocci,Vivian, Goulart,Antonio José, Polizeli,Maria de Lourdes Teixeira de Moraes, Monti,Rubens
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=S1517-83822006000300022
Resumo: Cyclodextrin glycosyltransferase (EC 2.4.1.19) is an enzyme that produces cyclodextrins from starch via an intramolecular transglycosylation reaction. An alkalophilic Bacillus strain, isolated from cassava peels, was identified as Bacillus licheniformis. CGTase production by this strain was better when potato starch was used as carbon source, followed by cassava starch and amylopectin. Glucose and amylose, on the other hand, acted as synthesis repressors. When the cultivation was supplemented with sodium ions and had the pH adjusted between 6.0 and 9.0, the microorganism maintained the growth and enzyme production capacity. This data is interesting because it contradicts the concept that alkalophilic microorganisms do not grow in this pH range. After ultrafiltration-centrifugation, one protein of 85.2 kDa with CGTase activity was isolated. This protein was identified in plates with starch and phenolphthalein. Determination of the optimum temperature showed higher activities at 25ºC and 55ºC, indicating the possible presence of more than one CGTase in the culture filtrate. Km and Vmax values were 1.77 mg/mL and 0.0263 U/mg protein, respectively, using potato starch as substrate.
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spelling Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its propertiescyclodextrin glycosyltransferaseCGTase productionBacilluslicheniformisBacillus beta-CDCyclodextrin glycosyltransferase (EC 2.4.1.19) is an enzyme that produces cyclodextrins from starch via an intramolecular transglycosylation reaction. An alkalophilic Bacillus strain, isolated from cassava peels, was identified as Bacillus licheniformis. CGTase production by this strain was better when potato starch was used as carbon source, followed by cassava starch and amylopectin. Glucose and amylose, on the other hand, acted as synthesis repressors. When the cultivation was supplemented with sodium ions and had the pH adjusted between 6.0 and 9.0, the microorganism maintained the growth and enzyme production capacity. This data is interesting because it contradicts the concept that alkalophilic microorganisms do not grow in this pH range. After ultrafiltration-centrifugation, one protein of 85.2 kDa with CGTase activity was isolated. This protein was identified in plates with starch and phenolphthalein. Determination of the optimum temperature showed higher activities at 25ºC and 55ºC, indicating the possible presence of more than one CGTase in the culture filtrate. Km and Vmax values were 1.77 mg/mL and 0.0263 U/mg protein, respectively, using potato starch as substrate.Sociedade Brasileira de Microbiologia2006-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822006000300022Brazilian Journal of Microbiology v.37 n.3 2006reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822006000300022info:eu-repo/semantics/openAccessBonilha,Paulo Roberto MartinsMenocci,VivianGoulart,Antonio JoséPolizeli,Maria de Lourdes Teixeira de MoraesMonti,Rubenseng2006-12-18T00:00:00Zoai:scielo:S1517-83822006000300022Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2006-12-18T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false
dc.title.none.fl_str_mv Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
title Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
spellingShingle Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
Bonilha,Paulo Roberto Martins
cyclodextrin glycosyltransferase
CGTase production
Bacilluslicheniformis
Bacillus beta-CD
title_short Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
title_full Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
title_fullStr Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
title_full_unstemmed Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
title_sort Cyclodextrin glycosyltransferase from Bacillus licheniformis: optimization of production and its properties
author Bonilha,Paulo Roberto Martins
author_facet Bonilha,Paulo Roberto Martins
Menocci,Vivian
Goulart,Antonio José
Polizeli,Maria de Lourdes Teixeira de Moraes
Monti,Rubens
author_role author
author2 Menocci,Vivian
Goulart,Antonio José
Polizeli,Maria de Lourdes Teixeira de Moraes
Monti,Rubens
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Bonilha,Paulo Roberto Martins
Menocci,Vivian
Goulart,Antonio José
Polizeli,Maria de Lourdes Teixeira de Moraes
Monti,Rubens
dc.subject.por.fl_str_mv cyclodextrin glycosyltransferase
CGTase production
Bacilluslicheniformis
Bacillus beta-CD
topic cyclodextrin glycosyltransferase
CGTase production
Bacilluslicheniformis
Bacillus beta-CD
description Cyclodextrin glycosyltransferase (EC 2.4.1.19) is an enzyme that produces cyclodextrins from starch via an intramolecular transglycosylation reaction. An alkalophilic Bacillus strain, isolated from cassava peels, was identified as Bacillus licheniformis. CGTase production by this strain was better when potato starch was used as carbon source, followed by cassava starch and amylopectin. Glucose and amylose, on the other hand, acted as synthesis repressors. When the cultivation was supplemented with sodium ions and had the pH adjusted between 6.0 and 9.0, the microorganism maintained the growth and enzyme production capacity. This data is interesting because it contradicts the concept that alkalophilic microorganisms do not grow in this pH range. After ultrafiltration-centrifugation, one protein of 85.2 kDa with CGTase activity was isolated. This protein was identified in plates with starch and phenolphthalein. Determination of the optimum temperature showed higher activities at 25ºC and 55ºC, indicating the possible presence of more than one CGTase in the culture filtrate. Km and Vmax values were 1.77 mg/mL and 0.0263 U/mg protein, respectively, using potato starch as substrate.
publishDate 2006
dc.date.none.fl_str_mv 2006-09-01
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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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822006000300022
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822006000300022
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1517-83822006000300022
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.37 n.3 2006
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
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