Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme

Detalhes bibliográficos
Autor(a) principal: Blanco, Kate Cristina [UNESP]
Data de Publicação: 2014
Outros Autores: Moraes, Flavio Faria de, Bernardi, Natalia Sozza [UNESP], Braga Vettori, Mary Helen Palmuti [UNESP], Monti, Rubens [UNESP], Contiero, Jonas [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://www.agriculturejournals.cz/web/cjfs.htm?volume=32&firstPage=48&type=publishedArticle
http://hdl.handle.net/11449/112758
Resumo: The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cydodextrin glycosyltransferase were 55 degrees C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.
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spelling Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzymecyclodextrin glycosyltransferaseaffinity chromatographypurificationThe properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cydodextrin glycosyltransferase were 55 degrees C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.UNESP Univ Estadual Paulista, Inst Biol Sci, Dept Biochem & Microbiol, BR-1515 Rio Claro, SP, BrazilUEM Univ Estadual Maringa, Dept Chem Engn, Maringa, Parana, BrazilUNESP Univ Estadual Paulista, Fac Pharmaceut Sci, Dept Food & Nutr, BR-1515 Rio Claro, SP, BrazilUNESP Univ Estadual Paulista, Inst Biol Sci, Dept Biochem & Microbiol, BR-1515 Rio Claro, SP, BrazilUNESP Univ Estadual Paulista, Fac Pharmaceut Sci, Dept Food & Nutr, BR-1515 Rio Claro, SP, BrazilCzech Academy Agricultural SciencesUniversidade Estadual Paulista (Unesp)Universidade Estadual de Maringá (UEM)Blanco, Kate Cristina [UNESP]Moraes, Flavio Faria deBernardi, Natalia Sozza [UNESP]Braga Vettori, Mary Helen Palmuti [UNESP]Monti, Rubens [UNESP]Contiero, Jonas [UNESP]2014-12-03T13:11:02Z2014-12-03T13:11:02Z2014-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article48-53application/pdfhttp://www.agriculturejournals.cz/web/cjfs.htm?volume=32&firstPage=48&type=publishedArticleCzech Journal of Food Sciences. Prague: Czech Academy Agricultural Sciences, v. 32, n. 1, p. 48-53, 2014.1212-1800http://hdl.handle.net/11449/112758WOS:000332595800007WOS000332595800007.pdf9859154979447005Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengCzech Journal Of Food Sciences0.8680,355info:eu-repo/semantics/openAccess2024-01-10T06:26:06Zoai:repositorio.unesp.br:11449/112758Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:37:08.770765Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
title Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
spellingShingle Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
Blanco, Kate Cristina [UNESP]
cyclodextrin glycosyltransferase
affinity chromatography
purification
title_short Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
title_full Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
title_fullStr Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
title_full_unstemmed Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
title_sort Cyclodextrin Production by Bacillus lehensis Isolated from Cassava Starch: Characterisation of a Novel Enzyme
author Blanco, Kate Cristina [UNESP]
author_facet Blanco, Kate Cristina [UNESP]
Moraes, Flavio Faria de
Bernardi, Natalia Sozza [UNESP]
Braga Vettori, Mary Helen Palmuti [UNESP]
Monti, Rubens [UNESP]
Contiero, Jonas [UNESP]
author_role author
author2 Moraes, Flavio Faria de
Bernardi, Natalia Sozza [UNESP]
Braga Vettori, Mary Helen Palmuti [UNESP]
Monti, Rubens [UNESP]
Contiero, Jonas [UNESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Universidade Estadual de Maringá (UEM)
dc.contributor.author.fl_str_mv Blanco, Kate Cristina [UNESP]
Moraes, Flavio Faria de
Bernardi, Natalia Sozza [UNESP]
Braga Vettori, Mary Helen Palmuti [UNESP]
Monti, Rubens [UNESP]
Contiero, Jonas [UNESP]
dc.subject.por.fl_str_mv cyclodextrin glycosyltransferase
affinity chromatography
purification
topic cyclodextrin glycosyltransferase
affinity chromatography
purification
description The properties of a previously unknown enzyme, denominated cyclodextrin glycosyltransferase, produced from Bacillus lehensis, were evaluated using affinity chromatography for protein purification. Enzyme characteristics (optimum pH and temperature; pH and temperature stability), the influence of substances on the enzyme activity, enzyme kinetics, and cyclodextrin production were analysed. Cyclodextrin glycosyltransferase was purified up to 320.74-fold by affinity chromatography using beta-cyclodextrin as the binder and it exhibited 8.71% activity recovery. This enzyme is a monomer with a molecular weight of 81.27 kDa, as estimated by SDS-PAGE. Optimum temperature and pH for cydodextrin glycosyltransferase were 55 degrees C and 8.0, respectively. The Michaelis-Menten constant was 8.62 g/l during maximum velocity of 0.858 g/l.h.
publishDate 2014
dc.date.none.fl_str_mv 2014-12-03T13:11:02Z
2014-12-03T13:11:02Z
2014-01-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.agriculturejournals.cz/web/cjfs.htm?volume=32&firstPage=48&type=publishedArticle
Czech Journal of Food Sciences. Prague: Czech Academy Agricultural Sciences, v. 32, n. 1, p. 48-53, 2014.
1212-1800
http://hdl.handle.net/11449/112758
WOS:000332595800007
WOS000332595800007.pdf
9859154979447005
url http://www.agriculturejournals.cz/web/cjfs.htm?volume=32&firstPage=48&type=publishedArticle
http://hdl.handle.net/11449/112758
identifier_str_mv Czech Journal of Food Sciences. Prague: Czech Academy Agricultural Sciences, v. 32, n. 1, p. 48-53, 2014.
1212-1800
WOS:000332595800007
WOS000332595800007.pdf
9859154979447005
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Czech Journal Of Food Sciences
0.868
0,355
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 48-53
application/pdf
dc.publisher.none.fl_str_mv Czech Academy Agricultural Sciences
publisher.none.fl_str_mv Czech Academy Agricultural Sciences
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808129444023369728

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