Influence of protein–pectin electrostatic interaction on the foam stability mechanism

Detalhes bibliográficos
Autor(a) principal: Sadahira, Mitie S. et al.
Data de Publicação: 2014
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório do Instituto de Tecnologia de Alimentos
Texto Completo: http://repositorio.ital.sp.gov.br/jspui/handle/123456789/495
Resumo: This study aimed at evaluating the effect of three independent variables: biopolymer concentration (egg white proteins and pectin) (2.0–4.0%, w/w); protein:pectin ratio (15:1–55:1); and temperature (70–80 ◦C), at pH 3.0, using a central composite design on the foaming properties (overrun, drainage and bubble growth rate). Foams produced with protein:pectin ratio 15:1 showed the lowest bubble growth rate and the greatest drainage, whereas protein:pectin ratio 55:1 presented the lowest drainage. Complexes obtained with protein:pectin ratio 15:1 were close to electroneutrality and showed larger size (95.91 ± 8.19 m) than those obtained with protein:pectin ratio 55:1 (45.92 ± 3.47 m) not electrically neutral. Larger particles seemed to build an interfacial viscoelastic network at the air–water interface with reduced gas permeability, leading to greater stability concerning the disproportionation. Soluble complexes of smaller sizes increased viscosity leading to a low drainage of liquid and inhibiting the bubbles coalescence.
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spelling Influence of protein–pectin electrostatic interaction on the foam stability mechanismElectrostatic interactionDisproportionationCoalescenceDrainageStabilityThis study aimed at evaluating the effect of three independent variables: biopolymer concentration (egg white proteins and pectin) (2.0–4.0%, w/w); protein:pectin ratio (15:1–55:1); and temperature (70–80 ◦C), at pH 3.0, using a central composite design on the foaming properties (overrun, drainage and bubble growth rate). Foams produced with protein:pectin ratio 15:1 showed the lowest bubble growth rate and the greatest drainage, whereas protein:pectin ratio 55:1 presented the lowest drainage. Complexes obtained with protein:pectin ratio 15:1 were close to electroneutrality and showed larger size (95.91 ± 8.19 m) than those obtained with protein:pectin ratio 55:1 (45.92 ± 3.47 m) not electrically neutral. Larger particles seemed to build an interfacial viscoelastic network at the air–water interface with reduced gas permeability, leading to greater stability concerning the disproportionation. Soluble complexes of smaller sizes increased viscosity leading to a low drainage of liquid and inhibiting the bubbles coalescence.ElsevierSadahira, Mitie S. et al.2022-10-07T19:33:45Z2022-10-07T19:33:45Z2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfCarbohydrate Polymers, v. 103, p. 55-61.http://repositorio.ital.sp.gov.br/jspui/handle/123456789/495reponame:Repositório do Instituto de Tecnologia de Alimentosinstname:Instituto de Tecnologia de Alimentos (ITAL)instacron:ITALenginfo:eu-repo/semantics/openAccess2022-10-07T19:33:47Zoai:http://repositorio.ital.sp.gov.br:123456789/495Repositório InstitucionalPUBhttp://repositorio.ital.sp.gov.br/oai/requestbjftsec@ital.sp.gov.br || bjftsec@ital.sp.gov.bropendoar:2022-10-07T19:33:47Repositório do Instituto de Tecnologia de Alimentos - Instituto de Tecnologia de Alimentos (ITAL)false
dc.title.none.fl_str_mv Influence of protein–pectin electrostatic interaction on the foam stability mechanism
title Influence of protein–pectin electrostatic interaction on the foam stability mechanism
spellingShingle Influence of protein–pectin electrostatic interaction on the foam stability mechanism
Sadahira, Mitie S. et al.
Electrostatic interaction
Disproportionation
Coalescence
Drainage
Stability
title_short Influence of protein–pectin electrostatic interaction on the foam stability mechanism
title_full Influence of protein–pectin electrostatic interaction on the foam stability mechanism
title_fullStr Influence of protein–pectin electrostatic interaction on the foam stability mechanism
title_full_unstemmed Influence of protein–pectin electrostatic interaction on the foam stability mechanism
title_sort Influence of protein–pectin electrostatic interaction on the foam stability mechanism
author Sadahira, Mitie S. et al.
author_facet Sadahira, Mitie S. et al.
author_role author
dc.contributor.none.fl_str_mv







dc.contributor.author.fl_str_mv Sadahira, Mitie S. et al.
dc.subject.none.fl_str_mv

dc.subject.por.fl_str_mv Electrostatic interaction
Disproportionation
Coalescence
Drainage
Stability
topic Electrostatic interaction
Disproportionation
Coalescence
Drainage
Stability
description This study aimed at evaluating the effect of three independent variables: biopolymer concentration (egg white proteins and pectin) (2.0–4.0%, w/w); protein:pectin ratio (15:1–55:1); and temperature (70–80 ◦C), at pH 3.0, using a central composite design on the foaming properties (overrun, drainage and bubble growth rate). Foams produced with protein:pectin ratio 15:1 showed the lowest bubble growth rate and the greatest drainage, whereas protein:pectin ratio 55:1 presented the lowest drainage. Complexes obtained with protein:pectin ratio 15:1 were close to electroneutrality and showed larger size (95.91 ± 8.19 m) than those obtained with protein:pectin ratio 55:1 (45.92 ± 3.47 m) not electrically neutral. Larger particles seemed to build an interfacial viscoelastic network at the air–water interface with reduced gas permeability, leading to greater stability concerning the disproportionation. Soluble complexes of smaller sizes increased viscosity leading to a low drainage of liquid and inhibiting the bubbles coalescence.
publishDate 2014
dc.date.none.fl_str_mv




2014
2022-10-07T19:33:45Z
2022-10-07T19:33:45Z
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.none.fl_str_mv

dc.identifier.uri.fl_str_mv Carbohydrate Polymers, v. 103, p. 55-61.
http://repositorio.ital.sp.gov.br/jspui/handle/123456789/495
identifier_str_mv
Carbohydrate Polymers, v. 103, p. 55-61.
url http://repositorio.ital.sp.gov.br/jspui/handle/123456789/495
dc.language.none.fl_str_mv
dc.language.iso.fl_str_mv eng
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language eng
dc.rights.none.fl_str_mv

dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
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application/pdf
dc.publisher.none.fl_str_mv

Elsevier
publisher.none.fl_str_mv

Elsevier
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reponame:Repositório do Instituto de Tecnologia de Alimentos
instname:Instituto de Tecnologia de Alimentos (ITAL)
instacron:ITAL
instname_str Instituto de Tecnologia de Alimentos (ITAL)
instacron_str ITAL
institution ITAL
reponame_str Repositório do Instituto de Tecnologia de Alimentos
collection Repositório do Instituto de Tecnologia de Alimentos
repository.name.fl_str_mv Repositório do Instituto de Tecnologia de Alimentos - Instituto de Tecnologia de Alimentos (ITAL)
repository.mail.fl_str_mv bjftsec@ital.sp.gov.br || bjftsec@ital.sp.gov.br
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