Influence of protein–pectin electrostatic interaction on the foam stability mechanism
Autor(a) principal: | |
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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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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 |
language_invalid_str_mv |
|
language |
eng |
dc.rights.none.fl_str_mv |
|
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
|
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
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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1813095546703839232 |