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Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business

[Image: see text] Proteins are known to be effective building blocks when it comes to structure formation in aqueous environments. Recently, we have shown that submicron colloidal protein particles can also be used to provide structure to liquid oil and form so-called oleogels ( A. de VriesJ. Colloi...

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Autores principales: de Vries, Auke, Lopez Gomez, Yuly, Jansen, Bas, van der Linden, Erik, Scholten, Elke
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2017
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364429/
https://www.ncbi.nlm.nih.gov/pubmed/28225592
http://dx.doi.org/10.1021/acsami.7b00443
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author de Vries, Auke
Lopez Gomez, Yuly
Jansen, Bas
van der Linden, Erik
Scholten, Elke
author_facet de Vries, Auke
Lopez Gomez, Yuly
Jansen, Bas
van der Linden, Erik
Scholten, Elke
author_sort de Vries, Auke
collection PubMed
description [Image: see text] Proteins are known to be effective building blocks when it comes to structure formation in aqueous environments. Recently, we have shown that submicron colloidal protein particles can also be used to provide structure to liquid oil and form so-called oleogels ( A. de VriesJ. Colloid Interface Sci.2017, 486, 75−83)27693552. To prevent particle agglomeration, a solvent exchange procedure was used to transfer the aggregates from water to the oil phase. The aim of the current paper was to elucidate on the enhanced stability against agglomeration of heat-set whey protein isolate (WPI) aggregates to develop an alternative for the solvent exchange procedure. Protein aggregates were transferred from water to several solvents differing in polarity to investigate the effect on agglomeration and changes in protein composition. We show that after drying protein aggregates by evaporation from solvents with a low polarity (e.g., hexane), the protein powder shows good dispersibility in liquid oil compared to powders dried from solvents with a high polarity. This difference in dispersibility could not be related to changes in protein composition or conformation but was instead related to the reduction of attractive capillary forces between the protein aggregates during drying. Following another route, agglomeration was also prevented by applying high freezing rates prior to freeze-drying. The rheological properties of the oleogels prepared with such freeze-dried protein aggregates were shown to be similar to that of oleogels prepared using a solvent exchange procedure. This Research Article provides valuable insights in how to tune the drying process to control protein agglomeration to allow for subsequent structure formation of proteins in liquid oil.
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spelling pubmed-53644292017-03-27 Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business de Vries, Auke Lopez Gomez, Yuly Jansen, Bas van der Linden, Erik Scholten, Elke ACS Appl Mater Interfaces [Image: see text] Proteins are known to be effective building blocks when it comes to structure formation in aqueous environments. Recently, we have shown that submicron colloidal protein particles can also be used to provide structure to liquid oil and form so-called oleogels ( A. de VriesJ. Colloid Interface Sci.2017, 486, 75−83)27693552. To prevent particle agglomeration, a solvent exchange procedure was used to transfer the aggregates from water to the oil phase. The aim of the current paper was to elucidate on the enhanced stability against agglomeration of heat-set whey protein isolate (WPI) aggregates to develop an alternative for the solvent exchange procedure. Protein aggregates were transferred from water to several solvents differing in polarity to investigate the effect on agglomeration and changes in protein composition. We show that after drying protein aggregates by evaporation from solvents with a low polarity (e.g., hexane), the protein powder shows good dispersibility in liquid oil compared to powders dried from solvents with a high polarity. This difference in dispersibility could not be related to changes in protein composition or conformation but was instead related to the reduction of attractive capillary forces between the protein aggregates during drying. Following another route, agglomeration was also prevented by applying high freezing rates prior to freeze-drying. The rheological properties of the oleogels prepared with such freeze-dried protein aggregates were shown to be similar to that of oleogels prepared using a solvent exchange procedure. This Research Article provides valuable insights in how to tune the drying process to control protein agglomeration to allow for subsequent structure formation of proteins in liquid oil. American Chemical Society 2017-02-22 2017-03-22 /pmc/articles/PMC5364429/ /pubmed/28225592 http://dx.doi.org/10.1021/acsami.7b00443 Text en Copyright © 2017 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes.
spellingShingle de Vries, Auke
Lopez Gomez, Yuly
Jansen, Bas
van der Linden, Erik
Scholten, Elke
Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business
title Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business
title_full Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business
title_fullStr Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business
title_full_unstemmed Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business
title_short Controlling Agglomeration of Protein Aggregates for Structure Formation in Liquid Oil: A Sticky Business
title_sort controlling agglomeration of protein aggregates for structure formation in liquid oil: a sticky business
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5364429/
https://www.ncbi.nlm.nih.gov/pubmed/28225592
http://dx.doi.org/10.1021/acsami.7b00443
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