Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties

The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in...

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Autores principales: Baeza, Rosa Isabel, Pilosof, Ana María Renata
Publicado: 2003
Materias:
Aggregation
Denaturation
Gelation
Kinetics
Thermodynamic incompatibility
Agglomeration
Gels
Heating
Proteins
Alcohols
alginic acid propylene glycol ester
beta lactoglobulin
polysaccharide
conference paper
food analysis
food processing
gel
gelation
kinetics
molecular dynamics
priority journal
protein aggregation
protein analysis
protein denaturation
protein interaction
protein structure
temperature
thermostability
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v31_n1-4_p81_Baeza
http://hdl.handle.net/20.500.12110/paper_09277765_v31_n1-4_p81_Baeza
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling paper:paper_09277765_v31_n1-4_p81_Baeza2023-06-08T15:52:06Z Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties Baeza, Rosa Isabel Pilosof, Ana María Renata Aggregation Denaturation Gelation Kinetics Thermodynamic incompatibility Agglomeration Gelation Gels Heating Proteins Denaturation Alcohols alginic acid propylene glycol ester beta lactoglobulin polysaccharide conference paper food analysis food processing gel gelation kinetics molecular dynamics priority journal protein aggregation protein analysis protein denaturation protein interaction protein structure temperature thermostability The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64-88°C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2-2.4°C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein-polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties. © 2003 Elsevier B.V. All rights reserved. Fil:Baeza, R. 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. 2003 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v31_n1-4_p81_Baeza http://hdl.handle.net/20.500.12110/paper_09277765_v31_n1-4_p81_Baeza
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Aggregation
Denaturation
Gelation
Kinetics
Thermodynamic incompatibility
Agglomeration
Gelation
Gels
Heating
Proteins
Denaturation
Alcohols
alginic acid propylene glycol ester
beta lactoglobulin
polysaccharide
conference paper
food analysis
food processing
gel
gelation
kinetics
molecular dynamics
priority journal
protein aggregation
protein analysis
protein denaturation
protein interaction
protein structure
temperature
thermostability
spellingShingle Aggregation
Denaturation
Gelation
Kinetics
Thermodynamic incompatibility
Agglomeration
Gelation
Gels
Heating
Proteins
Denaturation
Alcohols
alginic acid propylene glycol ester
beta lactoglobulin
polysaccharide
conference paper
food analysis
food processing
gel
gelation
kinetics
molecular dynamics
priority journal
protein aggregation
protein analysis
protein denaturation
protein interaction
protein structure
temperature
thermostability
Baeza, Rosa Isabel
Pilosof, Ana María Renata
Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
topic_facet Aggregation
Denaturation
Gelation
Kinetics
Thermodynamic incompatibility
Agglomeration
Gelation
Gels
Heating
Proteins
Denaturation
Alcohols
alginic acid propylene glycol ester
beta lactoglobulin
polysaccharide
conference paper
food analysis
food processing
gel
gelation
kinetics
molecular dynamics
priority journal
protein aggregation
protein analysis
protein denaturation
protein interaction
protein structure
temperature
thermostability
description The role of the non-gelling polysaccharide, propyleneglycol alginate (PGA), on the dynamics of gelation and gel properties of β-lactoglobulin (β-lg) under conditions where the protein alone does not gel (6%) was analyzed. To this end, the kinetics of gelation, aggregation and denaturation of β-lg in the mixed systems (pH 7) were studied at different temperatures (64-88°C). The presence of PGA increased thermal stability of β-lg. The rate of β-lg denaturation was decreased and the onset and peak denaturation temperatures increased by 2.2-2.4°C. PGA promoted the formation of larger aggregates that continued to grow in time. An average aggregate diameter of approximately 300 nm is reached at the gel point in the mixed β-lg+PGA systems, irrespective of the heating temperature. Comparing the activation energies for the aggregation (193 kJ/mol), denaturation (422 kJ/mol) and formation of the primary gel structure (1/tgel) (256 kJ/mol) processes in the mixed protein-polysaccharide system, it can be concluded that the rate determining step in the formation of the primary gel structure would be the aggregation of protein. Ea values for the processes after the gel point (solid phase gelation) suggest a diffusion limited process because of the high viscosity of the solid gelling matrix. The characteristics of the mixed β-lg+PGA gels in terms of rheological and textural parameters, water loss and microstructure were studied as a function of heating temperature and time. The extent of aggregation and the type of interactions involved, prior to denaturation seem to be very important in determining the gel structure and its properties. © 2003 Elsevier B.V. All rights reserved.
author Baeza, Rosa Isabel
Pilosof, Ana María Renata
author_facet Baeza, Rosa Isabel
Pilosof, Ana María Renata
author_sort Baeza, Rosa Isabel
title Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
title_short Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
title_full Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
title_fullStr Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
title_full_unstemmed Gelation of β-lactoglobulin in the presence of propylene glycol alginate: Kinetics and gel properties
title_sort gelation of β-lactoglobulin in the presence of propylene glycol alginate: kinetics and gel properties
publishDate 2003
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09277765_v31_n1-4_p81_Baeza
http://hdl.handle.net/20.500.12110/paper_09277765_v31_n1-4_p81_Baeza
work_keys_str_mv AT baezarosaisabel gelationofblactoglobulininthepresenceofpropyleneglycolalginatekineticsandgelproperties
AT pilosofanamariarenata gelationofblactoglobulininthepresenceofpropyleneglycolalginatekineticsandgelproperties
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