Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams

The aim of this work was to elucidate soy proteins-xanthan gum interactions at a molecular level by studying protein composition at the air-water interface of foams and in the solutions used to make them and to see if the different properties of heat denatured protein were reflected in the proportio...

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Autores principales: Carp, D.J., Bartholomai, G.B., Pilosof, A.M.R.
Formato: JOUR
Materias:
Foams
Interactions
Solutions
Soy protein
Xanthan
soybean protein
water
xanthan
air
article
densitometry
foam
molecular interaction
molecular weight
polyacrylamide gel electrophoresis
priority journal
protein denaturation
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_09277765_v12_n3-6_p309_Carp
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_09277765_v12_n3-6_p309_Carp
record_format dspace
spelling todo:paper_09277765_v12_n3-6_p309_Carp2023-10-03T15:47:11Z Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams Carp, D.J. Bartholomai, G.B. Pilosof, A.M.R. Foams Interactions Solutions Soy protein Xanthan soybean protein water xanthan air article densitometry foam molecular interaction molecular weight polyacrylamide gel electrophoresis priority journal protein denaturation The aim of this work was to elucidate soy proteins-xanthan gum interactions at a molecular level by studying protein composition at the air-water interface of foams and in the solutions used to make them and to see if the different properties of heat denatured protein were reflected in the proportions in which they were present at the interface or in the ability to interact with xanthan. To this end SDS-PAGE and densitometry was employed. Initial protein concentration and xanthan influenced the composition of proteins in the solutions used to make the foams. The increase in NSP concentration of solutions (0.5-6 wt.%) in the absence of xanthan promoted the formation of aggregates of low molecular weight (160 kDa), the association of A an B polypeptides and a decrease in α and α' subunits. As DSP concentration of solutions increased, an increase in the proportion of aggregates of high molecular weight (above 200 kDa) and B-polypeptide was observed. On addition of xanthan (0.025 and 0.05%) to protein solutions (0.5 and 2%), the formation of aggregates of high molecular weight was favoured for both NSP and DSP. In the absence of xanthan, no preferential adsorption of soy polypeptides was observed at the air-water interface of NSP foams. However in DSP foams, there was a preferential adsorption of B-polypeptides. Xanthan present in NSP foams (0.5 or 2%), caused an increase in the proportion of aggregates of high molecular weight at the interface as compared with the composition of solutions used to make the foams. An increase in proportion of AB-polypeptides (for 0.5% NSP and 0.025% xanthan) and B-polypeptides together with polypeptides of molecular weight lower than 14 kDa (for 0.5% NSP and 0.05% xanthan) was also observed at the interface in NSP foams. On the contrary, the presence of xanthan in DSP foams caused a decrease in the proportion of aggregates of high molecular weight and a concomitant increase in B-polypeptide. The B-11S polypeptide predominated the interface of DSP foams probably for its hydrophobicity and basic characteristics. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09277765_v12_n3-6_p309_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 Foams
Interactions
Solutions
Soy protein
Xanthan
soybean protein
water
xanthan
air
article
densitometry
foam
molecular interaction
molecular weight
polyacrylamide gel electrophoresis
priority journal
protein denaturation
spellingShingle Foams
Interactions
Solutions
Soy protein
Xanthan
soybean protein
water
xanthan
air
article
densitometry
foam
molecular interaction
molecular weight
polyacrylamide gel electrophoresis
priority journal
protein denaturation
Carp, D.J.
Bartholomai, G.B.
Pilosof, A.M.R.
Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
topic_facet Foams
Interactions
Solutions
Soy protein
Xanthan
soybean protein
water
xanthan
air
article
densitometry
foam
molecular interaction
molecular weight
polyacrylamide gel electrophoresis
priority journal
protein denaturation
description The aim of this work was to elucidate soy proteins-xanthan gum interactions at a molecular level by studying protein composition at the air-water interface of foams and in the solutions used to make them and to see if the different properties of heat denatured protein were reflected in the proportions in which they were present at the interface or in the ability to interact with xanthan. To this end SDS-PAGE and densitometry was employed. Initial protein concentration and xanthan influenced the composition of proteins in the solutions used to make the foams. The increase in NSP concentration of solutions (0.5-6 wt.%) in the absence of xanthan promoted the formation of aggregates of low molecular weight (160 kDa), the association of A an B polypeptides and a decrease in α and α' subunits. As DSP concentration of solutions increased, an increase in the proportion of aggregates of high molecular weight (above 200 kDa) and B-polypeptide was observed. On addition of xanthan (0.025 and 0.05%) to protein solutions (0.5 and 2%), the formation of aggregates of high molecular weight was favoured for both NSP and DSP. In the absence of xanthan, no preferential adsorption of soy polypeptides was observed at the air-water interface of NSP foams. However in DSP foams, there was a preferential adsorption of B-polypeptides. Xanthan present in NSP foams (0.5 or 2%), caused an increase in the proportion of aggregates of high molecular weight at the interface as compared with the composition of solutions used to make the foams. An increase in proportion of AB-polypeptides (for 0.5% NSP and 0.025% xanthan) and B-polypeptides together with polypeptides of molecular weight lower than 14 kDa (for 0.5% NSP and 0.05% xanthan) was also observed at the interface in NSP foams. On the contrary, the presence of xanthan in DSP foams caused a decrease in the proportion of aggregates of high molecular weight and a concomitant increase in B-polypeptide. The B-11S polypeptide predominated the interface of DSP foams probably for its hydrophobicity and basic characteristics.
format JOUR
author Carp, D.J.
Bartholomai, G.B.
Pilosof, A.M.R.
author_facet Carp, D.J.
Bartholomai, G.B.
Pilosof, A.M.R.
author_sort Carp, D.J.
title Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
title_short Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
title_full Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
title_fullStr Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
title_full_unstemmed Electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
title_sort electrophoretic studies for determining soy proteins-xanthan gum interactions in foams
url http://hdl.handle.net/20.500.12110/paper_09277765_v12_n3-6_p309_Carp
work_keys_str_mv AT carpdj electrophoreticstudiesfordeterminingsoyproteinsxanthanguminteractionsinfoams
AT bartholomaigb electrophoreticstudiesfordeterminingsoyproteinsxanthanguminteractionsinfoams
AT pilosofamr electrophoreticstudiesfordeterminingsoyproteinsxanthanguminteractionsinfoams
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