Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin

Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both...

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Detalles Bibliográficos
Autor principal:	Pilosof, Ana María Renata
Publicado:	2007
Materias:	Coacervate Denaturation Differential scanning calorimetry Gels Protein polysaccharide interactions
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v21_n8_p1344_Capitani http://hdl.handle.net/20.500.12110/paper_0268005X_v21_n8_p1344_Capitani
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_0268005X_v21_n8_p1344_Capitani
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spelling	paper:paper_0268005X_v21_n8_p1344_Capitani2023-06-08T15:23:44Z Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin Pilosof, Ana María Renata Coacervate Denaturation Differential scanning calorimetry Gels Protein polysaccharide interactions Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both complexes showed a maximum stability at pH 4, that is close to the pH of obtention of β-lg/CMC coacervate (pH 4) and α-lac/CMC coacervate (pH 3.2). Protein complexation increased the thermostability of β-lg by approximately 6-8 °C and that of α-lac by approximately 26 °C due to immobilization of protein molecules in a complex, mainly by electrostatic interactions and because of different amounts of bound polysaccharide. The denaturation enthalpy of complexed proteins markedly decreased as compared to free proteins. Storage modulus (G′) and loss modulus (G″) were recorded to reflect the structure development during heating β-lg/CMC and α-lac/CMC complexes at different pH values. β-lg/CMC complex at 20 wt% was a viscoelastic liquid at pH values within 2 and 8 but upon heating turned to a particulate viscoelastic gel. However, α-lac/CMC complex formed before heating opaque, large visible white particulate aggregates that sticked together to give a solid viscoelastic structure that was not further modified by thermal processing. © 2006 Elsevier Ltd. All rights reserved. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v21_n8_p1344_Capitani http://hdl.handle.net/20.500.12110/paper_0268005X_v21_n8_p1344_Capitani
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Coacervate Denaturation Differential scanning calorimetry Gels Protein polysaccharide interactions
spellingShingle	Coacervate Denaturation Differential scanning calorimetry Gels Protein polysaccharide interactions Pilosof, Ana María Renata Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
topic_facet	Coacervate Denaturation Differential scanning calorimetry Gels Protein polysaccharide interactions
description	Thermostability and gelation of the main proteins of whey, α-lactalbumin (α-lac) and β-lactoglobulin (β-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both complexes showed a maximum stability at pH 4, that is close to the pH of obtention of β-lg/CMC coacervate (pH 4) and α-lac/CMC coacervate (pH 3.2). Protein complexation increased the thermostability of β-lg by approximately 6-8 °C and that of α-lac by approximately 26 °C due to immobilization of protein molecules in a complex, mainly by electrostatic interactions and because of different amounts of bound polysaccharide. The denaturation enthalpy of complexed proteins markedly decreased as compared to free proteins. Storage modulus (G′) and loss modulus (G″) were recorded to reflect the structure development during heating β-lg/CMC and α-lac/CMC complexes at different pH values. β-lg/CMC complex at 20 wt% was a viscoelastic liquid at pH values within 2 and 8 but upon heating turned to a particulate viscoelastic gel. However, α-lac/CMC complex formed before heating opaque, large visible white particulate aggregates that sticked together to give a solid viscoelastic structure that was not further modified by thermal processing. © 2006 Elsevier Ltd. All rights reserved.
author	Pilosof, Ana María Renata
author_facet	Pilosof, Ana María Renata
author_sort	Pilosof, Ana María Renata
title	Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
title_short	Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
title_full	Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
title_fullStr	Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
title_full_unstemmed	Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
title_sort	influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin
publishDate	2007
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v21_n8_p1344_Capitani http://hdl.handle.net/20.500.12110/paper_0268005X_v21_n8_p1344_Capitani
work_keys_str_mv	AT pilosofanamariarenata influenceofcomplexingcarboxymethylcelluloseonthethermostabilityandgelationofalactalbuminandblactoglobulin
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Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin

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