Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties

Detalhes bibliográficos
Autor(a) principal: Santos, Igor José Boggione
Data de Publicação: 2019
Outros Autores: Hernandez, Héctor Luís Hernandez, Costa, Mariana Helena Cardoso, Lafetá Júnior, José Antônio de Queiroz, Coimbra, Jane Sélia dos Reis
Tipo de documento: Artigo
Idioma: por
Título da fonte: LOCUS Repositório Institucional da UFV
Texto Completo: https://doi.org/10.1016/j.foodres.2018.08.065
http://www.locus.ufv.br/handle/123456789/24022
Resumo: Conjugates of protein (α-lactalbumin, β-lactoglobulin, and lysozyme) with polysaccharides (guar, locust, pectin, and carboxymethilcellulose) were prepared via Maillard reaction by the dry-heating method. The conjugates were characterizated by using the browning index, extent of reaction, grafting degree, sodium dodecyl sulfate – polyacrilamide gel electrophoresis, fluorescence, and circular dichroism. The emulsifying properties and foaming ability of the formed conjugates were also evaluated. Conjugates with pectin and Lz-CMC system showed an increase in the browning index with the increase of the heating time. Circular dichroism and fluorescence data pointed out to conformational changes of proteins during glycation. The lysozyme (lz) conjugates presented the highest degree of glycation (89.1%). The α-Lactalbumin (α-la) - polysaccharides (PS) conjugates showed foam stability higher than the mixture (α-la + PS), the pure α-la, and the conjugates of β-lactoglobulin (β-lg) and lysozyme (lz) for all studied time (30, 60, and 120 min). The α-la-carboxymethylcellulose (CMC) conjugate presented the highest value of foaming stability (85.71). The pure β-lg shows greater foam stability and volume than β-lg-PS conjugates and mixture (β-lg + PS). The lz conjugates do not exihibit foam stability, except for the lz-CMC conjugate that showed stability up to 60 min. Furthermore, emulsion stability of the systems was affected by sonication time. Conjugates of α-la have greatly potencial applications as novel foaming agents in food industry.
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spelling Santos, Igor José BoggioneHernandez, Héctor Luís HernandezCosta, Mariana Helena CardosoLafetá Júnior, José Antônio de QueirozCoimbra, Jane Sélia dos Reis2019-03-20T17:33:30Z2019-03-20T17:33:30Z2019-020963-9969https://doi.org/10.1016/j.foodres.2018.08.065http://www.locus.ufv.br/handle/123456789/24022Conjugates of protein (α-lactalbumin, β-lactoglobulin, and lysozyme) with polysaccharides (guar, locust, pectin, and carboxymethilcellulose) were prepared via Maillard reaction by the dry-heating method. The conjugates were characterizated by using the browning index, extent of reaction, grafting degree, sodium dodecyl sulfate – polyacrilamide gel electrophoresis, fluorescence, and circular dichroism. The emulsifying properties and foaming ability of the formed conjugates were also evaluated. Conjugates with pectin and Lz-CMC system showed an increase in the browning index with the increase of the heating time. Circular dichroism and fluorescence data pointed out to conformational changes of proteins during glycation. The lysozyme (lz) conjugates presented the highest degree of glycation (89.1%). The α-Lactalbumin (α-la) - polysaccharides (PS) conjugates showed foam stability higher than the mixture (α-la + PS), the pure α-la, and the conjugates of β-lactoglobulin (β-lg) and lysozyme (lz) for all studied time (30, 60, and 120 min). The α-la-carboxymethylcellulose (CMC) conjugate presented the highest value of foaming stability (85.71). The pure β-lg shows greater foam stability and volume than β-lg-PS conjugates and mixture (β-lg + PS). The lz conjugates do not exihibit foam stability, except for the lz-CMC conjugate that showed stability up to 60 min. Furthermore, emulsion stability of the systems was affected by sonication time. Conjugates of α-la have greatly potencial applications as novel foaming agents in food industry.porFood Research InternationalVolume 116, Pages 492-498, February 2019Elsevier B. V.info:eu-repo/semantics/openAccessEmulsifying propertiesGlycosylationFoaming propertiesProteinMaillard reactionConjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional propertiesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf1163150https://locus.ufv.br//bitstream/123456789/24022/1/artigo.pdfa98d0de765d2878908b1d49293f26c2fMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/24022/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52123456789/240222019-03-20 14:41:03.752oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452019-03-20T17:41:03LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false
dc.title.en.fl_str_mv Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
title Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
spellingShingle Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
Santos, Igor José Boggione
Emulsifying properties
Glycosylation
Foaming properties
Protein
Maillard reaction
title_short Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
title_full Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
title_fullStr Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
title_full_unstemmed Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
title_sort Conjugates of α-lactalbumin, β-lactoglobulin, and lysozyme with polysaccharides: Characterization and techno-functional properties
author Santos, Igor José Boggione
author_facet Santos, Igor José Boggione
Hernandez, Héctor Luís Hernandez
Costa, Mariana Helena Cardoso
Lafetá Júnior, José Antônio de Queiroz
Coimbra, Jane Sélia dos Reis
author_role author
author2 Hernandez, Héctor Luís Hernandez
Costa, Mariana Helena Cardoso
Lafetá Júnior, José Antônio de Queiroz
Coimbra, Jane Sélia dos Reis
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Santos, Igor José Boggione
Hernandez, Héctor Luís Hernandez
Costa, Mariana Helena Cardoso
Lafetá Júnior, José Antônio de Queiroz
Coimbra, Jane Sélia dos Reis
dc.subject.pt-BR.fl_str_mv Emulsifying properties
Glycosylation
Foaming properties
Protein
Maillard reaction
topic Emulsifying properties
Glycosylation
Foaming properties
Protein
Maillard reaction
description Conjugates of protein (α-lactalbumin, β-lactoglobulin, and lysozyme) with polysaccharides (guar, locust, pectin, and carboxymethilcellulose) were prepared via Maillard reaction by the dry-heating method. The conjugates were characterizated by using the browning index, extent of reaction, grafting degree, sodium dodecyl sulfate – polyacrilamide gel electrophoresis, fluorescence, and circular dichroism. The emulsifying properties and foaming ability of the formed conjugates were also evaluated. Conjugates with pectin and Lz-CMC system showed an increase in the browning index with the increase of the heating time. Circular dichroism and fluorescence data pointed out to conformational changes of proteins during glycation. The lysozyme (lz) conjugates presented the highest degree of glycation (89.1%). The α-Lactalbumin (α-la) - polysaccharides (PS) conjugates showed foam stability higher than the mixture (α-la + PS), the pure α-la, and the conjugates of β-lactoglobulin (β-lg) and lysozyme (lz) for all studied time (30, 60, and 120 min). The α-la-carboxymethylcellulose (CMC) conjugate presented the highest value of foaming stability (85.71). The pure β-lg shows greater foam stability and volume than β-lg-PS conjugates and mixture (β-lg + PS). The lz conjugates do not exihibit foam stability, except for the lz-CMC conjugate that showed stability up to 60 min. Furthermore, emulsion stability of the systems was affected by sonication time. Conjugates of α-la have greatly potencial applications as novel foaming agents in food industry.
publishDate 2019
dc.date.accessioned.fl_str_mv 2019-03-20T17:33:30Z
dc.date.available.fl_str_mv 2019-03-20T17:33:30Z
dc.date.issued.fl_str_mv 2019-02
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 https://doi.org/10.1016/j.foodres.2018.08.065
http://www.locus.ufv.br/handle/123456789/24022
dc.identifier.issn.none.fl_str_mv 0963-9969
identifier_str_mv 0963-9969
url https://doi.org/10.1016/j.foodres.2018.08.065
http://www.locus.ufv.br/handle/123456789/24022
dc.language.iso.fl_str_mv por
language por
dc.relation.ispartofseries.pt-BR.fl_str_mv Volume 116, Pages 492-498, February 2019
dc.rights.driver.fl_str_mv Elsevier B. V.
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Elsevier B. V.
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Food Research International
publisher.none.fl_str_mv Food Research International
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