Impact of proteins-κ-carrageenan interactions on foam properties

Foaming properties of κ-carrageenan (κ-C)+β-lactoglobulin (β-lg), native and denatured soy protein and the thermal stability of foams were investigated. Apparent viscosity measurements were used to obtain the gelation rate and maximum viscosity of foams. Gelling and melting temperatures of the solut...

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Autores principales: Carp, Dina Judith, Baeza, Rosa Isabel, Pilosof, Ana María Renata
Publicado: 2004
Materias:
β-Lactoglobulin
κ-Carrageenan
Foam stability
Soy protein
Glycine max
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v37_n5_p573_Carp
http://hdl.handle.net/20.500.12110/paper_00236438_v37_n5_p573_Carp
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_00236438_v37_n5_p573_Carp
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spelling paper:paper_00236438_v37_n5_p573_Carp2023-06-08T14:51:41Z Impact of proteins-κ-carrageenan interactions on foam properties Carp, Dina Judith Baeza, Rosa Isabel Pilosof, Ana María Renata β-Lactoglobulin κ-Carrageenan Foam stability Soy protein Glycine max Foaming properties of κ-carrageenan (κ-C)+β-lactoglobulin (β-lg), native and denatured soy protein and the thermal stability of foams were investigated. Apparent viscosity measurements were used to obtain the gelation rate and maximum viscosity of foams. Gelling and melting temperatures of the solutions determined by dynamic rheology were related to the thermal stability of foams. Foam expansion of the mixed κ-C+ protein solutions followed the same order as the pure protein solutions (β-lg>DSP>NSP). However, the presence of κ-C reduced foam expansion due to the higher viscosity of the systems. No liquid drainage or collapse was observed while apparent viscosity was measured. DSP induced a greater synergistic effect with κ-C, reflected in a faster gelling rate and increased foam stability. The thermal stability of foams stored at temperatures between 5°C and 45°C showed significant differences when they were pre-gelled at 5°C. A large increase in foam stability was observed at 25°C, which is above the average T gel and below the melting temperatures of the systems. The kinetic analysis of the process revealed that different mechanisms were involved in the drainage of pre-gelled or non-gelled foams. © 2004 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved. Fil:Carp, D.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Baeza, R.I. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2004 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v37_n5_p573_Carp http://hdl.handle.net/20.500.12110/paper_00236438_v37_n5_p573_Carp
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic β-Lactoglobulin
κ-Carrageenan
Foam stability
Soy protein
Glycine max
spellingShingle β-Lactoglobulin
κ-Carrageenan
Foam stability
Soy protein
Glycine max
Carp, Dina Judith
Baeza, Rosa Isabel
Pilosof, Ana María Renata
Impact of proteins-κ-carrageenan interactions on foam properties
topic_facet β-Lactoglobulin
κ-Carrageenan
Foam stability
Soy protein
Glycine max
description Foaming properties of κ-carrageenan (κ-C)+β-lactoglobulin (β-lg), native and denatured soy protein and the thermal stability of foams were investigated. Apparent viscosity measurements were used to obtain the gelation rate and maximum viscosity of foams. Gelling and melting temperatures of the solutions determined by dynamic rheology were related to the thermal stability of foams. Foam expansion of the mixed κ-C+ protein solutions followed the same order as the pure protein solutions (β-lg>DSP>NSP). However, the presence of κ-C reduced foam expansion due to the higher viscosity of the systems. No liquid drainage or collapse was observed while apparent viscosity was measured. DSP induced a greater synergistic effect with κ-C, reflected in a faster gelling rate and increased foam stability. The thermal stability of foams stored at temperatures between 5°C and 45°C showed significant differences when they were pre-gelled at 5°C. A large increase in foam stability was observed at 25°C, which is above the average T gel and below the melting temperatures of the systems. The kinetic analysis of the process revealed that different mechanisms were involved in the drainage of pre-gelled or non-gelled foams. © 2004 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved.
author Carp, Dina Judith
Baeza, Rosa Isabel
Pilosof, Ana María Renata
author_facet Carp, Dina Judith
Baeza, Rosa Isabel
Pilosof, Ana María Renata
author_sort Carp, Dina Judith
title Impact of proteins-κ-carrageenan interactions on foam properties
title_short Impact of proteins-κ-carrageenan interactions on foam properties
title_full Impact of proteins-κ-carrageenan interactions on foam properties
title_fullStr Impact of proteins-κ-carrageenan interactions on foam properties
title_full_unstemmed Impact of proteins-κ-carrageenan interactions on foam properties
title_sort impact of proteins-κ-carrageenan interactions on foam properties
publishDate 2004
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v37_n5_p573_Carp
http://hdl.handle.net/20.500.12110/paper_00236438_v37_n5_p573_Carp
work_keys_str_mv AT carpdinajudith impactofproteinskcarrageenaninteractionsonfoamproperties
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