Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes

Detalhes bibliográficos
Autor(a) principal: Adalberto, P. R.
Data de Publicação: 2006
Outros Autores: Massabni, A. C., Goulart, A. J., Contiero, J., Carmona, E. C., Cardello, L., Monti, R.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1385/ABAB:133:2:163
http://hdl.handle.net/11449/231012
Resumo: Trichoderma reesei FTKO-39 grown at 35°C for 5 d on wheat bran supplemented with MgCl2 and lactose as the carbon source produced two isozymes of β-galactosidase: BGT I and BGT II. These isozymes were partially purified on a DEAE-Trisacryl column. Both BGT I and BGT II fractions exhibited optimum activity at 65°C, but the pH optima were 4.0 and 6.5, respectively. The isozymes also showed similar thermal stability. However, BGT I was more stable than BGT II in a pH range of 3.0-10.0. At least two different β-galactosidases are produced by T. reesei, as revealed by the two bands seen on a 6% polyacrylamide gel stained for activity. Copyright © 2006 by Humana Press Inc. All rights of any nature whatsoever reserved.
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spelling Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymesβ-GalactosidaseIsozymesPartial purificationSemisolid fermentationTrichoderma reeseiTrichoderma reesei FTKO-39 grown at 35°C for 5 d on wheat bran supplemented with MgCl2 and lactose as the carbon source produced two isozymes of β-galactosidase: BGT I and BGT II. These isozymes were partially purified on a DEAE-Trisacryl column. Both BGT I and BGT II fractions exhibited optimum activity at 65°C, but the pH optima were 4.0 and 6.5, respectively. The isozymes also showed similar thermal stability. However, BGT I was more stable than BGT II in a pH range of 3.0-10.0. At least two different β-galactosidases are produced by T. reesei, as revealed by the two bands seen on a 6% polyacrylamide gel stained for activity. Copyright © 2006 by Humana Press Inc. All rights of any nature whatsoever reserved.Department of General Inorganic and Chemistry Institute of Chemistry, Rua Prof. Francisco Degni, s/n, 14800-900, Araraquara, SPDepartment of Biochemistry and Technological Chemistry Institute of Chemistry, Rua Prof. Francisco Degni, s/n, 14800-900, Araraquara, SPDepartment of Biochemistry and Microbiology Institute of Biosciences, Avenida 24-A, 1515, 13506-900, Rio Claro, SPDepartment of Food and Nutrition School of Pharmaceutical Sciences, Rodovia Araraquara-Jaú Km1, 14801-902, Araraquara, SPInstitute of ChemistryInstitute of BiosciencesSchool of Pharmaceutical SciencesAdalberto, P. R.Massabni, A. C.Goulart, A. J.Contiero, J.Carmona, E. C.Cardello, L.Monti, R.2022-04-29T08:43:14Z2022-04-29T08:43:14Z2006-05-31info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article163-170http://dx.doi.org/10.1385/ABAB:133:2:163Applied Biochemistry and Biotechnology, v. 133, n. 2, p. 163-170, 2006.0273-2289http://hdl.handle.net/11449/23101210.1385/ABAB:133:2:1632-s2.0-33646894664Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengApplied Biochemistry and Biotechnologyinfo:eu-repo/semantics/openAccess2024-06-21T12:47:24Zoai:repositorio.unesp.br:11449/231012Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:49:19.020322Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
title Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
spellingShingle Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
Adalberto, P. R.
β-Galactosidase
Isozymes
Partial purification
Semisolid fermentation
Trichoderma reesei
title_short Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
title_full Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
title_fullStr Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
title_full_unstemmed Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
title_sort Production of β-galactosidase by Trichoderma reesei FTKO-39 in wheat bran: Partial purification of two isozymes
author Adalberto, P. R.
author_facet Adalberto, P. R.
Massabni, A. C.
Goulart, A. J.
Contiero, J.
Carmona, E. C.
Cardello, L.
Monti, R.
author_role author
author2 Massabni, A. C.
Goulart, A. J.
Contiero, J.
Carmona, E. C.
Cardello, L.
Monti, R.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Institute of Chemistry
Institute of Biosciences
School of Pharmaceutical Sciences
dc.contributor.author.fl_str_mv Adalberto, P. R.
Massabni, A. C.
Goulart, A. J.
Contiero, J.
Carmona, E. C.
Cardello, L.
Monti, R.
dc.subject.por.fl_str_mv β-Galactosidase
Isozymes
Partial purification
Semisolid fermentation
Trichoderma reesei
topic β-Galactosidase
Isozymes
Partial purification
Semisolid fermentation
Trichoderma reesei
description Trichoderma reesei FTKO-39 grown at 35°C for 5 d on wheat bran supplemented with MgCl2 and lactose as the carbon source produced two isozymes of β-galactosidase: BGT I and BGT II. These isozymes were partially purified on a DEAE-Trisacryl column. Both BGT I and BGT II fractions exhibited optimum activity at 65°C, but the pH optima were 4.0 and 6.5, respectively. The isozymes also showed similar thermal stability. However, BGT I was more stable than BGT II in a pH range of 3.0-10.0. At least two different β-galactosidases are produced by T. reesei, as revealed by the two bands seen on a 6% polyacrylamide gel stained for activity. Copyright © 2006 by Humana Press Inc. All rights of any nature whatsoever reserved.
publishDate 2006
dc.date.none.fl_str_mv 2006-05-31
2022-04-29T08:43:14Z
2022-04-29T08:43:14Z
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://dx.doi.org/10.1385/ABAB:133:2:163
Applied Biochemistry and Biotechnology, v. 133, n. 2, p. 163-170, 2006.
0273-2289
http://hdl.handle.net/11449/231012
10.1385/ABAB:133:2:163
2-s2.0-33646894664
url http://dx.doi.org/10.1385/ABAB:133:2:163
http://hdl.handle.net/11449/231012
identifier_str_mv Applied Biochemistry and Biotechnology, v. 133, n. 2, p. 163-170, 2006.
0273-2289
10.1385/ABAB:133:2:163
2-s2.0-33646894664
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Applied Biochemistry and Biotechnology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 163-170
dc.source.none.fl_str_mv Scopus
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_ 1808129555791085568

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