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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Autores principales:	Capitani, C., Pérez, Oscar.E., Pacheco, B., Teresa, M., Pilosof, A.M.R.
Formato:	JOUR
Materias:	Coacervate Denaturation Differential scanning calorimetry Gels Protein polysaccharide interactions
Acceso en línea:	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	todo:paper_0268005X_v21_n8_p1344_Capitani
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spelling	todo:paper_0268005X_v21_n8_p1344_Capitani2023-10-03T15:13:36Z Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin Capitani, C. Pérez, Oscar.E. Pacheco, B. Teresa, M. Pilosof, A.M.R. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Capitani, C. Pérez, Oscar.E. Pacheco, B. Teresa, M. Pilosof, A.M.R. 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.
format	JOUR
author	Capitani, C. Pérez, Oscar.E. Pacheco, B. Teresa, M. Pilosof, A.M.R.
author_facet	Capitani, C. Pérez, Oscar.E. Pacheco, B. Teresa, M. Pilosof, A.M.R.
author_sort	Capitani, C.
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
url	http://hdl.handle.net/20.500.12110/paper_0268005X_v21_n8_p1344_Capitani
work_keys_str_mv	AT capitanic influenceofcomplexingcarboxymethylcelluloseonthethermostabilityandgelationofalactalbuminandblactoglobulin AT perezoscare influenceofcomplexingcarboxymethylcelluloseonthethermostabilityandgelationofalactalbuminandblactoglobulin AT pachecob influenceofcomplexingcarboxymethylcelluloseonthethermostabilityandgelationofalactalbuminandblactoglobulin AT teresam influenceofcomplexingcarboxymethylcelluloseonthethermostabilityandgelationofalactalbuminandblactoglobulin AT pilosofamr influenceofcomplexingcarboxymethylcelluloseonthethermostabilityandgelationofalactalbuminandblactoglobulin
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Influence of complexing carboxymethylcellulose on the thermostability and gelation of α-lactalbumin and β-lactoglobulin

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