Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality

Autores
Steffolani, Maria Eugenia; Ribotta, Pablo Daniel; Pérez, Gabriela Teresa; León, Alberto E.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glucose oxidase (Gox), transglutaminase (TG), and pentosanase (Pn) were investigated for their effect on bread quality. The changes introduced in wheat protein by the action of these enzymes were analysed to explain dough behaviour. Gox treatment decreased free sulphydryl groups (SHf), increased glutenin macropolymer contents, and modified the electrophoretic pattern of protein fractions. Gox modified mainly albumin, globulin, and glutenin, forming large protein aggregates. These modifications explained the high strength of the dough and the low bread specific volume of samples with Gox. TG treatment modified solubility in SDS of protein and decreased glutenin macropolymer content. However, it formed large protein aggregates. The new cross-linking bonds introduced by this enzyme were different to S-S bonds and, consequently, the dough was less extensible and showed high resistance. Pn treatment increased water soluble pentosan content. Moreover, in these samples a tendency to increase SHf content was observed. In addition, Pn increased protein solubility in isopropanol, which indicates that the reduction of pentosans size decreases steric impediment of insoluble pentosans, thus increasing interaction among protein and making their extraction easier. These changes at the microscopic level allowed explaining the formation of softer dough and the production of higher specific volume in breads with Pn.
Fil: Steffolani, Maria Eugenia. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Ribotta, Pablo Daniel. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Pérez, Gabriela Teresa. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina
Fil: León, Alberto E.. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina
Materia
BREAD
GLUCOSE OXIDASE
PENTOSANASE
TRANSGLUTAMINASE
WHEAT PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/130255
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/130255
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making qualitySteffolani, Maria EugeniaRibotta, Pablo DanielPérez, Gabriela TeresaLeón, Alberto E.BREADGLUCOSE OXIDASEPENTOSANASETRANSGLUTAMINASEWHEAT PROTEINhttps://purl.org/becyt/ford/4.5https://purl.org/becyt/ford/4Glucose oxidase (Gox), transglutaminase (TG), and pentosanase (Pn) were investigated for their effect on bread quality. The changes introduced in wheat protein by the action of these enzymes were analysed to explain dough behaviour. Gox treatment decreased free sulphydryl groups (SHf), increased glutenin macropolymer contents, and modified the electrophoretic pattern of protein fractions. Gox modified mainly albumin, globulin, and glutenin, forming large protein aggregates. These modifications explained the high strength of the dough and the low bread specific volume of samples with Gox. TG treatment modified solubility in SDS of protein and decreased glutenin macropolymer content. However, it formed large protein aggregates. The new cross-linking bonds introduced by this enzyme were different to S-S bonds and, consequently, the dough was less extensible and showed high resistance. Pn treatment increased water soluble pentosan content. Moreover, in these samples a tendency to increase SHf content was observed. In addition, Pn increased protein solubility in isopropanol, which indicates that the reduction of pentosans size decreases steric impediment of insoluble pentosans, thus increasing interaction among protein and making their extraction easier. These changes at the microscopic level allowed explaining the formation of softer dough and the production of higher specific volume in breads with Pn.Fil: Steffolani, Maria Eugenia. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaFil: Ribotta, Pablo Daniel. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaFil: Pérez, Gabriela Teresa. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; ArgentinaFil: León, Alberto E.. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; ArgentinaAcademic Press Ltd - Elsevier Science Ltd2010-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/130255Steffolani, Maria Eugenia; Ribotta, Pablo Daniel; Pérez, Gabriela Teresa; León, Alberto E.; Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality; Academic Press Ltd - Elsevier Science Ltd; Journal of Cereal Science; 51; 3; 5-2010; 366-3730733-5210CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0733521010000342info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jcs.2010.01.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:52:40Zoai:ri.conicet.gov.ar:11336/130255instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:52:41.295CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
title Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
spellingShingle Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
Steffolani, Maria Eugenia
BREAD
GLUCOSE OXIDASE
PENTOSANASE
TRANSGLUTAMINASE
WHEAT PROTEIN
title_short Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
title_full Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
title_fullStr Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
title_full_unstemmed Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
title_sort Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality
dc.creator.none.fl_str_mv Steffolani, Maria Eugenia
Ribotta, Pablo Daniel
Pérez, Gabriela Teresa
León, Alberto E.
author Steffolani, Maria Eugenia
author_facet Steffolani, Maria Eugenia
Ribotta, Pablo Daniel
Pérez, Gabriela Teresa
León, Alberto E.
author_role author
author2 Ribotta, Pablo Daniel
Pérez, Gabriela Teresa
León, Alberto E.
author2_role author
author
author
dc.subject.none.fl_str_mv BREAD
GLUCOSE OXIDASE
PENTOSANASE
TRANSGLUTAMINASE
WHEAT PROTEIN
topic BREAD
GLUCOSE OXIDASE
PENTOSANASE
TRANSGLUTAMINASE
WHEAT PROTEIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.5
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv Glucose oxidase (Gox), transglutaminase (TG), and pentosanase (Pn) were investigated for their effect on bread quality. The changes introduced in wheat protein by the action of these enzymes were analysed to explain dough behaviour. Gox treatment decreased free sulphydryl groups (SHf), increased glutenin macropolymer contents, and modified the electrophoretic pattern of protein fractions. Gox modified mainly albumin, globulin, and glutenin, forming large protein aggregates. These modifications explained the high strength of the dough and the low bread specific volume of samples with Gox. TG treatment modified solubility in SDS of protein and decreased glutenin macropolymer content. However, it formed large protein aggregates. The new cross-linking bonds introduced by this enzyme were different to S-S bonds and, consequently, the dough was less extensible and showed high resistance. Pn treatment increased water soluble pentosan content. Moreover, in these samples a tendency to increase SHf content was observed. In addition, Pn increased protein solubility in isopropanol, which indicates that the reduction of pentosans size decreases steric impediment of insoluble pentosans, thus increasing interaction among protein and making their extraction easier. These changes at the microscopic level allowed explaining the formation of softer dough and the production of higher specific volume in breads with Pn.
Fil: Steffolani, Maria Eugenia. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Ribotta, Pablo Daniel. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Pérez, Gabriela Teresa. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina
Fil: León, Alberto E.. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias; Argentina
description Glucose oxidase (Gox), transglutaminase (TG), and pentosanase (Pn) were investigated for their effect on bread quality. The changes introduced in wheat protein by the action of these enzymes were analysed to explain dough behaviour. Gox treatment decreased free sulphydryl groups (SHf), increased glutenin macropolymer contents, and modified the electrophoretic pattern of protein fractions. Gox modified mainly albumin, globulin, and glutenin, forming large protein aggregates. These modifications explained the high strength of the dough and the low bread specific volume of samples with Gox. TG treatment modified solubility in SDS of protein and decreased glutenin macropolymer content. However, it formed large protein aggregates. The new cross-linking bonds introduced by this enzyme were different to S-S bonds and, consequently, the dough was less extensible and showed high resistance. Pn treatment increased water soluble pentosan content. Moreover, in these samples a tendency to increase SHf content was observed. In addition, Pn increased protein solubility in isopropanol, which indicates that the reduction of pentosans size decreases steric impediment of insoluble pentosans, thus increasing interaction among protein and making their extraction easier. These changes at the microscopic level allowed explaining the formation of softer dough and the production of higher specific volume in breads with Pn.
publishDate 2010
dc.date.none.fl_str_mv 2010-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/130255
Steffolani, Maria Eugenia; Ribotta, Pablo Daniel; Pérez, Gabriela Teresa; León, Alberto E.; Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality; Academic Press Ltd - Elsevier Science Ltd; Journal of Cereal Science; 51; 3; 5-2010; 366-373
0733-5210
CONICET Digital
CONICET
url http://hdl.handle.net/11336/130255
identifier_str_mv Steffolani, Maria Eugenia; Ribotta, Pablo Daniel; Pérez, Gabriela Teresa; León, Alberto E.; Effect of glucose oxidase, transglutaminase, and pentosanase on wheat proteins: Relationship with dough properties and bread-making quality; Academic Press Ltd - Elsevier Science Ltd; Journal of Cereal Science; 51; 3; 5-2010; 366-373
0733-5210
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0733521010000342
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jcs.2010.01.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Ltd - Elsevier Science Ltd
publisher.none.fl_str_mv Academic Press Ltd - Elsevier Science Ltd
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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