Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | por eng |
Título da fonte: | Acta scientiarum. Technology (Online) |
Texto Completo: | http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944 |
Resumo: | The cyclodextrins (CDs) are cyclic maltooligosaccharides obtained by cyclization of linear chains of starch, catalyzed by the enzyme cyclomaltodextringlucanotransferase (CGTase). The interest in CD production results from the formation of inclusion complexes, which allow many important applications, especially in food, pharmaceutical and cosmetic industries. The substances complexed generally have their properties modified by complexation. It is appreciated if increased solubility and higher thermal and chemical stabilities are obtained. In this work, a kinetic model was developed for the production of cyclodextrins in the presence of CGTase from alkalophilic Bacillus sp., taking into account the reversibility of the cyclization reaction, the simultaneous production of b and g-CD and also the inhibitory influence of the substrate and products (CDs), on the enzymatic activity of the CGTase. The substrate formed from a solution of maltodextrins was treated as a single substrate. The model was compared with experimental results of 24h of reaction and this comparison demonstrated that there was a very good representation of the data throughout the test period. The model also allowed explaining the observation of different experimental values for each Michaelis-Menten constant and substrate inhibition constant for each CD, although the CDs are produced from the same substrate. |
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Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944cyclic oligosaccharidescyclizationenzyme kineticsinclusion complexesintramolecular transglycosylationProcessos BioquimicosThe cyclodextrins (CDs) are cyclic maltooligosaccharides obtained by cyclization of linear chains of starch, catalyzed by the enzyme cyclomaltodextringlucanotransferase (CGTase). The interest in CD production results from the formation of inclusion complexes, which allow many important applications, especially in food, pharmaceutical and cosmetic industries. The substances complexed generally have their properties modified by complexation. It is appreciated if increased solubility and higher thermal and chemical stabilities are obtained. In this work, a kinetic model was developed for the production of cyclodextrins in the presence of CGTase from alkalophilic Bacillus sp., taking into account the reversibility of the cyclization reaction, the simultaneous production of b and g-CD and also the inhibitory influence of the substrate and products (CDs), on the enzymatic activity of the CGTase. The substrate formed from a solution of maltodextrins was treated as a single substrate. The model was compared with experimental results of 24h of reaction and this comparison demonstrated that there was a very good representation of the data throughout the test period. The model also allowed explaining the observation of different experimental values for each Michaelis-Menten constant and substrate inhibition constant for each CD, although the CDs are produced from the same substrate. Universidade Estadual De Maringá2013-05-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionCinética enzimáticaapplication/pdfapplication/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/1394410.4025/actascitechnol.v35i4.13944Acta Scientiarum. Technology; Vol 35 No 4 (2013); 687-693Acta Scientiarum. Technology; v. 35 n. 4 (2013); 687-6931806-25631807-8664reponame:Acta scientiarum. Technology (Online)instname:Universidade Estadual de Maringá (UEM)instacron:UEMporenghttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944/pdfhttp://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944/pdf_1De Souza, MarcosFaria, Sérgio Henrique Bernardo deZanin, Gisella MariaMoraes, Flavio Fariainfo:eu-repo/semantics/openAccess2024-05-17T13:03:26Zoai:periodicos.uem.br/ojs:article/13944Revistahttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/indexPUBhttps://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/oai||actatech@uem.br1807-86641806-2563opendoar:2024-05-17T13:03:26Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM)false |
dc.title.none.fl_str_mv |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
title |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
spellingShingle |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 De Souza, Marcos cyclic oligosaccharides cyclization enzyme kinetics inclusion complexes intramolecular transglycosylation Processos Bioquimicos |
title_short |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
title_full |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
title_fullStr |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
title_full_unstemmed |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
title_sort |
Kinetics of the simultaneous production of b- and g-cyclodextrins catalyzed by CGTase from alkalophilic Bacillus sp. - doi: 10.4025/actascitechnol.v35i4.13944 |
author |
De Souza, Marcos |
author_facet |
De Souza, Marcos Faria, Sérgio Henrique Bernardo de Zanin, Gisella Maria Moraes, Flavio Faria |
author_role |
author |
author2 |
Faria, Sérgio Henrique Bernardo de Zanin, Gisella Maria Moraes, Flavio Faria |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
De Souza, Marcos Faria, Sérgio Henrique Bernardo de Zanin, Gisella Maria Moraes, Flavio Faria |
dc.subject.por.fl_str_mv |
cyclic oligosaccharides cyclization enzyme kinetics inclusion complexes intramolecular transglycosylation Processos Bioquimicos |
topic |
cyclic oligosaccharides cyclization enzyme kinetics inclusion complexes intramolecular transglycosylation Processos Bioquimicos |
description |
The cyclodextrins (CDs) are cyclic maltooligosaccharides obtained by cyclization of linear chains of starch, catalyzed by the enzyme cyclomaltodextringlucanotransferase (CGTase). The interest in CD production results from the formation of inclusion complexes, which allow many important applications, especially in food, pharmaceutical and cosmetic industries. The substances complexed generally have their properties modified by complexation. It is appreciated if increased solubility and higher thermal and chemical stabilities are obtained. In this work, a kinetic model was developed for the production of cyclodextrins in the presence of CGTase from alkalophilic Bacillus sp., taking into account the reversibility of the cyclization reaction, the simultaneous production of b and g-CD and also the inhibitory influence of the substrate and products (CDs), on the enzymatic activity of the CGTase. The substrate formed from a solution of maltodextrins was treated as a single substrate. The model was compared with experimental results of 24h of reaction and this comparison demonstrated that there was a very good representation of the data throughout the test period. The model also allowed explaining the observation of different experimental values for each Michaelis-Menten constant and substrate inhibition constant for each CD, although the CDs are produced from the same substrate. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-05-22 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Cinética enzimática |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944 10.4025/actascitechnol.v35i4.13944 |
url |
http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944 |
identifier_str_mv |
10.4025/actascitechnol.v35i4.13944 |
dc.language.iso.fl_str_mv |
por eng |
language |
por eng |
dc.relation.none.fl_str_mv |
http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944/pdf http://www.periodicos.uem.br/ojs/index.php/ActaSciTechnol/article/view/13944/pdf_1 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Estadual De Maringá |
publisher.none.fl_str_mv |
Universidade Estadual De Maringá |
dc.source.none.fl_str_mv |
Acta Scientiarum. Technology; Vol 35 No 4 (2013); 687-693 Acta Scientiarum. Technology; v. 35 n. 4 (2013); 687-693 1806-2563 1807-8664 reponame:Acta scientiarum. Technology (Online) instname:Universidade Estadual de Maringá (UEM) instacron:UEM |
instname_str |
Universidade Estadual de Maringá (UEM) |
instacron_str |
UEM |
institution |
UEM |
reponame_str |
Acta scientiarum. Technology (Online) |
collection |
Acta scientiarum. Technology (Online) |
repository.name.fl_str_mv |
Acta scientiarum. Technology (Online) - Universidade Estadual de Maringá (UEM) |
repository.mail.fl_str_mv |
||actatech@uem.br |
_version_ |
1799315334388252672 |