Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/j.carbpol.2014.11.060 http://www.locus.ufv.br/handle/123456789/19460 |
Resumo: | Protein–polysaccharide conjugates often display improved techno-functional properties when compared to their individual involved biomolecules. α-Lactalbumin:acacia gum (α-la:AG) conjugates were prepared via Maillard reaction by the dry-heating method. Conjugate formation was confirmed using results of absorbance, o-phthalaldehyde test, sodium dodecyl sulfate–polyacrilamide gel electrophoresis (SDS–PAGE) and size exclusion chromatography. Techno-functional properties (emulsifying characteristics, solubility, and thermal stability) were evaluated for α-la, α-la/AG mixtures and α-la:AG conjugates. Conjugate thermal stability was improved compared to pure α-la treated at the same conditions of conjugate formation. Response surface methodology was used to establish models to predict solubility and emulsifying activity as functions of the salt concentration, pH and reaction time. α-la:AG conjugate solubility is affected in a complex manner by the three factors analyzed. Emulsifying activity index (EAI) of α-la is significantly affected by pH, while the α-la:AG EAI is affected by the three analyzed factors. Both solubility and EAI are maximized with pH 8.0, NaCl concentration of 0.3 mol L−1 and two days of Maillard reaction. |
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Oliveira, Fabíola Cristina deCoimbra, Jane Sélia dos ReisOliveira, Eduardo Basílio deRodrigues, Marina Quadrio Raposo BrancoSabioni, Rachel CamposSouza, Bartolomeu Warlene Silva deSantos, Igor José Boggione2018-05-10T16:29:37Z2018-05-10T16:29:37Z2014-12-0501448617https://doi.org/10.1016/j.carbpol.2014.11.060http://www.locus.ufv.br/handle/123456789/19460Protein–polysaccharide conjugates often display improved techno-functional properties when compared to their individual involved biomolecules. α-Lactalbumin:acacia gum (α-la:AG) conjugates were prepared via Maillard reaction by the dry-heating method. Conjugate formation was confirmed using results of absorbance, o-phthalaldehyde test, sodium dodecyl sulfate–polyacrilamide gel electrophoresis (SDS–PAGE) and size exclusion chromatography. Techno-functional properties (emulsifying characteristics, solubility, and thermal stability) were evaluated for α-la, α-la/AG mixtures and α-la:AG conjugates. Conjugate thermal stability was improved compared to pure α-la treated at the same conditions of conjugate formation. Response surface methodology was used to establish models to predict solubility and emulsifying activity as functions of the salt concentration, pH and reaction time. α-la:AG conjugate solubility is affected in a complex manner by the three factors analyzed. Emulsifying activity index (EAI) of α-la is significantly affected by pH, while the α-la:AG EAI is affected by the three analyzed factors. Both solubility and EAI are maximized with pH 8.0, NaCl concentration of 0.3 mol L−1 and two days of Maillard reaction.engCarbohydrate Polymersv. 119, p. 210-218, March 2015Elsevier Ltdinfo:eu-repo/semantics/openAccessEmulsifying propertiesGlycosylationSolubilityThermal stabilityWhey proteinAcacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumininfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf3138732https://locus.ufv.br//bitstream/123456789/19460/1/artigo.pdfe884292f45c95c800d194849299ace0bMD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/19460/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg4638https://locus.ufv.br//bitstream/123456789/19460/3/artigo.pdf.jpg66f6a95860b67bb7b67561646036f8e2MD53123456789/194602018-05-10 23:00:58.897oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-05-11T02:00:58LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
title |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
spellingShingle |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin Oliveira, Fabíola Cristina de Emulsifying properties Glycosylation Solubility Thermal stability Whey protein |
title_short |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
title_full |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
title_fullStr |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
title_full_unstemmed |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
title_sort |
Acacia gum as modifier of thermal stability, solubility and emulsifying properties of α-lactalbumin |
author |
Oliveira, Fabíola Cristina de |
author_facet |
Oliveira, Fabíola Cristina de Coimbra, Jane Sélia dos Reis Oliveira, Eduardo Basílio de Rodrigues, Marina Quadrio Raposo Branco Sabioni, Rachel Campos Souza, Bartolomeu Warlene Silva de Santos, Igor José Boggione |
author_role |
author |
author2 |
Coimbra, Jane Sélia dos Reis Oliveira, Eduardo Basílio de Rodrigues, Marina Quadrio Raposo Branco Sabioni, Rachel Campos Souza, Bartolomeu Warlene Silva de Santos, Igor José Boggione |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Oliveira, Fabíola Cristina de Coimbra, Jane Sélia dos Reis Oliveira, Eduardo Basílio de Rodrigues, Marina Quadrio Raposo Branco Sabioni, Rachel Campos Souza, Bartolomeu Warlene Silva de Santos, Igor José Boggione |
dc.subject.pt-BR.fl_str_mv |
Emulsifying properties Glycosylation Solubility Thermal stability Whey protein |
topic |
Emulsifying properties Glycosylation Solubility Thermal stability Whey protein |
description |
Protein–polysaccharide conjugates often display improved techno-functional properties when compared to their individual involved biomolecules. α-Lactalbumin:acacia gum (α-la:AG) conjugates were prepared via Maillard reaction by the dry-heating method. Conjugate formation was confirmed using results of absorbance, o-phthalaldehyde test, sodium dodecyl sulfate–polyacrilamide gel electrophoresis (SDS–PAGE) and size exclusion chromatography. Techno-functional properties (emulsifying characteristics, solubility, and thermal stability) were evaluated for α-la, α-la/AG mixtures and α-la:AG conjugates. Conjugate thermal stability was improved compared to pure α-la treated at the same conditions of conjugate formation. Response surface methodology was used to establish models to predict solubility and emulsifying activity as functions of the salt concentration, pH and reaction time. α-la:AG conjugate solubility is affected in a complex manner by the three factors analyzed. Emulsifying activity index (EAI) of α-la is significantly affected by pH, while the α-la:AG EAI is affected by the three analyzed factors. Both solubility and EAI are maximized with pH 8.0, NaCl concentration of 0.3 mol L−1 and two days of Maillard reaction. |
publishDate |
2014 |
dc.date.issued.fl_str_mv |
2014-12-05 |
dc.date.accessioned.fl_str_mv |
2018-05-10T16:29:37Z |
dc.date.available.fl_str_mv |
2018-05-10T16:29:37Z |
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.carbpol.2014.11.060 http://www.locus.ufv.br/handle/123456789/19460 |
dc.identifier.issn.none.fl_str_mv |
01448617 |
identifier_str_mv |
01448617 |
url |
https://doi.org/10.1016/j.carbpol.2014.11.060 http://www.locus.ufv.br/handle/123456789/19460 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 119, p. 210-218, March 2015 |
dc.rights.driver.fl_str_mv |
Elsevier Ltd info:eu-repo/semantics/openAccess |
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Elsevier Ltd |
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openAccess |
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dc.publisher.none.fl_str_mv |
Carbohydrate Polymers |
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Carbohydrate Polymers |
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