Production of whey protein-based aggregates under ohmic heating

Detalhes bibliográficos
Autor(a) principal: Pereira, Ricardo
Data de Publicação: 2016
Outros Autores: Rodrigues, Rui M., Ramos, Óscar L., Malcata, F. X., Teixeira, J. A., Vicente, A. A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/41300
Resumo: Formation of whey protein isolate protein aggregates under the influence of moderate electric fields upon ohmic heating (OH) has been monitored through evaluation of molecular protein unfolding, loss of its solubility, and aggregation. To shed more light on the microstructure of the protein aggregates produced by OH, samples were assayed by transmission electron microscopy (TEM). Results show that during early steps of an OH thermal treatment, aggregation of whey proteins can be reduced with a concomitant reduction of the heating chargeby reducing the come-up time (CUT) needed to reach a target temperatureand increase of the electric field applied (from 6 to 12 V cm1). Exposure of reactive free thiol groups involved in molecular unfolding of -lactoglobulin (-lg) can be reduced from 10 to 20 %, when a CUT of 10 s is combined with an electric field of 12 V cm1. Kinetic and multivariate analysis evidenced that the presence of an electric field during heating contributes to a change in the amplitude of aggregation, as well as in the shape of the produced aggregates. TEM discloses the appearance of small fibrillar aggregates upon the influence of OH, which have recognized potential in the functionalization of food protein networks. This study demonstrated that OH technology can be used to tailor denaturation and aggregation behavior of whey proteins due to the presence of a constant electric field together with the ability to provide a very fast heating, thus overcoming heat transfer limitations that naturally occur during conventional thermal treatments.
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spelling Production of whey protein-based aggregates under ohmic heatingWhey protein isolateOhmic heatingElectric fieldsProtein solubilityAggregation kineticsProtein fibrillar aggregatesScience & TechnologyFormation of whey protein isolate protein aggregates under the influence of moderate electric fields upon ohmic heating (OH) has been monitored through evaluation of molecular protein unfolding, loss of its solubility, and aggregation. To shed more light on the microstructure of the protein aggregates produced by OH, samples were assayed by transmission electron microscopy (TEM). Results show that during early steps of an OH thermal treatment, aggregation of whey proteins can be reduced with a concomitant reduction of the heating chargeby reducing the come-up time (CUT) needed to reach a target temperatureand increase of the electric field applied (from 6 to 12 V cm1). Exposure of reactive free thiol groups involved in molecular unfolding of -lactoglobulin (-lg) can be reduced from 10 to 20 %, when a CUT of 10 s is combined with an electric field of 12 V cm1. Kinetic and multivariate analysis evidenced that the presence of an electric field during heating contributes to a change in the amplitude of aggregation, as well as in the shape of the produced aggregates. TEM discloses the appearance of small fibrillar aggregates upon the influence of OH, which have recognized potential in the functionalization of food protein networks. This study demonstrated that OH technology can be used to tailor denaturation and aggregation behavior of whey proteins due to the presence of a constant electric field together with the ability to provide a very fast heating, thus overcoming heat transfer limitations that naturally occur during conventional thermal treatments.The authors thank the Portuguese Foundation for Science and Technology (FCT) strategic project UID/BIO/04469/2013 unit, the project RECI/BBB-EBI/0179/2012 (FCOMP-01-0124FEDER-027462), and the project BBioInd - Biotechnology and Bioengineering for improved Industrial and Agro-Food processes^ REF. NORTE-07-0124-FEDER-000028 co-funded by the Programa Operacional Regional do Norte(ON.2–O Novo Norte), QREN, FEDER. The authors would like to acknowledge Rui Fernandes from the Institute for Molecular and Cell Biology (IBMC), University of Porto, for the assistance in taking the TEM pictures. The authors Ricardo N. Pereira and Oscar L. Ramos also acknowledge FCT for their post-doctoral grants with references SFRH/BPD/81887/2011 and SFRH/BPD/80766/2011, respectively.Springer VerlagUniversidade do MinhoPereira, RicardoRodrigues, Rui M.Ramos, Óscar L.Malcata, F. X.Teixeira, J. A.Vicente, A. A.2016-042016-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/41300engPereira, Ricardo; Rodrigues, Rui M.; Ramos, Óscar L.; Malcata, F. X.; Teixeira, J. A.; Vicente, A. A., Production of whey protein-based aggregates under ohmic heating. Food and Bioprocess Technology, 9(4), 576-587, 20161935-51301935-514910.1007/s11947-015-1651-4http://www.springer.com/food+science/journal/11947info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-11T04:11:35Zoai:repositorium.sdum.uminho.pt:1822/41300Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-11T04:11:35Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Production of whey protein-based aggregates under ohmic heating
title Production of whey protein-based aggregates under ohmic heating
spellingShingle Production of whey protein-based aggregates under ohmic heating
Pereira, Ricardo
Whey protein isolate
Ohmic heating
Electric fields
Protein solubility
Aggregation kinetics
Protein fibrillar aggregates
Science & Technology
title_short Production of whey protein-based aggregates under ohmic heating
title_full Production of whey protein-based aggregates under ohmic heating
title_fullStr Production of whey protein-based aggregates under ohmic heating
title_full_unstemmed Production of whey protein-based aggregates under ohmic heating
title_sort Production of whey protein-based aggregates under ohmic heating
author Pereira, Ricardo
author_facet Pereira, Ricardo
Rodrigues, Rui M.
Ramos, Óscar L.
Malcata, F. X.
Teixeira, J. A.
Vicente, A. A.
author_role author
author2 Rodrigues, Rui M.
Ramos, Óscar L.
Malcata, F. X.
Teixeira, J. A.
Vicente, A. A.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Pereira, Ricardo
Rodrigues, Rui M.
Ramos, Óscar L.
Malcata, F. X.
Teixeira, J. A.
Vicente, A. A.
dc.subject.por.fl_str_mv Whey protein isolate
Ohmic heating
Electric fields
Protein solubility
Aggregation kinetics
Protein fibrillar aggregates
Science & Technology
topic Whey protein isolate
Ohmic heating
Electric fields
Protein solubility
Aggregation kinetics
Protein fibrillar aggregates
Science & Technology
description Formation of whey protein isolate protein aggregates under the influence of moderate electric fields upon ohmic heating (OH) has been monitored through evaluation of molecular protein unfolding, loss of its solubility, and aggregation. To shed more light on the microstructure of the protein aggregates produced by OH, samples were assayed by transmission electron microscopy (TEM). Results show that during early steps of an OH thermal treatment, aggregation of whey proteins can be reduced with a concomitant reduction of the heating chargeby reducing the come-up time (CUT) needed to reach a target temperatureand increase of the electric field applied (from 6 to 12 V cm1). Exposure of reactive free thiol groups involved in molecular unfolding of -lactoglobulin (-lg) can be reduced from 10 to 20 %, when a CUT of 10 s is combined with an electric field of 12 V cm1. Kinetic and multivariate analysis evidenced that the presence of an electric field during heating contributes to a change in the amplitude of aggregation, as well as in the shape of the produced aggregates. TEM discloses the appearance of small fibrillar aggregates upon the influence of OH, which have recognized potential in the functionalization of food protein networks. This study demonstrated that OH technology can be used to tailor denaturation and aggregation behavior of whey proteins due to the presence of a constant electric field together with the ability to provide a very fast heating, thus overcoming heat transfer limitations that naturally occur during conventional thermal treatments.
publishDate 2016
dc.date.none.fl_str_mv 2016-04
2016-04-01T00:00:00Z
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://hdl.handle.net/1822/41300
url http://hdl.handle.net/1822/41300
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Pereira, Ricardo; Rodrigues, Rui M.; Ramos, Óscar L.; Malcata, F. X.; Teixeira, J. A.; Vicente, A. A., Production of whey protein-based aggregates under ohmic heating. Food and Bioprocess Technology, 9(4), 576-587, 2016
1935-5130
1935-5149
10.1007/s11947-015-1651-4
http://www.springer.com/food+science/journal/11947
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer Verlag
publisher.none.fl_str_mv Springer Verlag
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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