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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/130255
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:20:03Zoai: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:34982025-09-29 10:20:03.857CONICET 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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1844614177354678272 |
score |
13.070432 |