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Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel

In this work, by means of complex physicochemical methods the structural features of a composite κ-carrageenan–gelatin system were studied in comparison with initial protein gel. The correlation between the morphology of hydrogels and their mechanical properties was demonstrated through the example...

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Autores principales: Makarova, Anastasiya O., Derkach, Svetlana R., Kadyirov, Aidar I., Ziganshina, Sufia A., Kazantseva, Mariia A., Zueva, Olga S., Gubaidullin, Aidar T., Zuev, Yuriy F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9612265/
https://www.ncbi.nlm.nih.gov/pubmed/36297925
http://dx.doi.org/10.3390/polym14204347
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author Makarova, Anastasiya O.
Derkach, Svetlana R.
Kadyirov, Aidar I.
Ziganshina, Sufia A.
Kazantseva, Mariia A.
Zueva, Olga S.
Gubaidullin, Aidar T.
Zuev, Yuriy F.
author_facet Makarova, Anastasiya O.
Derkach, Svetlana R.
Kadyirov, Aidar I.
Ziganshina, Sufia A.
Kazantseva, Mariia A.
Zueva, Olga S.
Gubaidullin, Aidar T.
Zuev, Yuriy F.
author_sort Makarova, Anastasiya O.
collection PubMed
description In this work, by means of complex physicochemical methods the structural features of a composite κ-carrageenan–gelatin system were studied in comparison with initial protein gel. The correlation between the morphology of hydrogels and their mechanical properties was demonstrated through the example of changes in their rheological characteristics. The experiments carried out with PXRD, SAXS, AFM and rheology approaches gave new information on the structure and mechanical performance of κ-carrageenan–gelatin hydrogel. The combination of PXRD, SAXS and AFM results showed that the morphological structures of individual components were not observed in the composite protein–polysaccharide hydrogels. The results of the mechanical testing of initial gelatin and engineered κ-carrageenan–gelatin gel showed the substantially denser parking of polymer chains in the composite system due to a significant increase in intermolecular protein–polysaccharide contacts. Close results were indirectly followed from the SAXS estimations—the driving force for the formation of the common supramolecular structural arrangement of proteins and polysaccharides was the increase in the density of network of macromolecular chains entanglements; therefore, an increase in the energy costs was necessary to change the conformational rearrangements of the studied system. This increase in the macromolecular arrangement led to the growth of the supramolecular associate size and the growth of interchain physical bonds. This led to an increase in the composite gel plasticity, whereas the enlargement of scattering particles made the novel gel system not only more rigid, but also more fragile.
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spelling pubmed-96122652022-10-28 Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel Makarova, Anastasiya O. Derkach, Svetlana R. Kadyirov, Aidar I. Ziganshina, Sufia A. Kazantseva, Mariia A. Zueva, Olga S. Gubaidullin, Aidar T. Zuev, Yuriy F. Polymers (Basel) Article In this work, by means of complex physicochemical methods the structural features of a composite κ-carrageenan–gelatin system were studied in comparison with initial protein gel. The correlation between the morphology of hydrogels and their mechanical properties was demonstrated through the example of changes in their rheological characteristics. The experiments carried out with PXRD, SAXS, AFM and rheology approaches gave new information on the structure and mechanical performance of κ-carrageenan–gelatin hydrogel. The combination of PXRD, SAXS and AFM results showed that the morphological structures of individual components were not observed in the composite protein–polysaccharide hydrogels. The results of the mechanical testing of initial gelatin and engineered κ-carrageenan–gelatin gel showed the substantially denser parking of polymer chains in the composite system due to a significant increase in intermolecular protein–polysaccharide contacts. Close results were indirectly followed from the SAXS estimations—the driving force for the formation of the common supramolecular structural arrangement of proteins and polysaccharides was the increase in the density of network of macromolecular chains entanglements; therefore, an increase in the energy costs was necessary to change the conformational rearrangements of the studied system. This increase in the macromolecular arrangement led to the growth of the supramolecular associate size and the growth of interchain physical bonds. This led to an increase in the composite gel plasticity, whereas the enlargement of scattering particles made the novel gel system not only more rigid, but also more fragile. MDPI 2022-10-15 /pmc/articles/PMC9612265/ /pubmed/36297925 http://dx.doi.org/10.3390/polym14204347 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Makarova, Anastasiya O.
Derkach, Svetlana R.
Kadyirov, Aidar I.
Ziganshina, Sufia A.
Kazantseva, Mariia A.
Zueva, Olga S.
Gubaidullin, Aidar T.
Zuev, Yuriy F.
Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel
title Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel
title_full Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel
title_fullStr Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel
title_full_unstemmed Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel
title_short Supramolecular Structure and Mechanical Performance of κ-Carrageenan–Gelatin Gel
title_sort supramolecular structure and mechanical performance of κ-carrageenan–gelatin gel
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9612265/
https://www.ncbi.nlm.nih.gov/pubmed/36297925
http://dx.doi.org/10.3390/polym14204347
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