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Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment
The impact of key classes of compounds found in wine on protein removal by the ion-exchange resin, Macro-Prep(®) High S, was examined by adsorption isotherm experiments. A model wine system, which contained a prototypical protein Bovine Serum Albumin (BSA), was used. We systematically changed concen...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8272113/ https://www.ncbi.nlm.nih.gov/pubmed/34206735 http://dx.doi.org/10.3390/molecules26133905 |
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author | Sun, Lin Srinivas, Ananya Runnebaum, Ron C. |
author_facet | Sun, Lin Srinivas, Ananya Runnebaum, Ron C. |
author_sort | Sun, Lin |
collection | PubMed |
description | The impact of key classes of compounds found in wine on protein removal by the ion-exchange resin, Macro-Prep(®) High S, was examined by adsorption isotherm experiments. A model wine system, which contained a prototypical protein Bovine Serum Albumin (BSA), was used. We systematically changed concentrations of individual chemical components to generate and compare adsorption isotherm plots and to quantify adsorption affinity or capacity parameters of Macro-Prep(®) High S ion-exchange resin. The pH (hydronium ion concentration), ethanol concentration, and prototypical phenolics and polysaccharide compounds are known to impact interactions with proteins and thus could alter the adsorption affinity and capacity of Macro-Prep(®) High S ion-exchange resin. At low equilibrium protein concentrations (< ~0.3 (g BSA)/L) and at high equilibrium protein concentrations in model wines at various pH, the adsorption behavior followed the Langmuir isotherm, most likely due to the resin acting as a monolayer adsorbent. The resulting range of BSA capacity was between 0.15–0.18 (g BSA)/(g Macro-Prep(®) High S resin). With the addition of ethanol, catechin, caffeic acid, and polysaccharides, the protein adsorption behavior was observed to differ at higher equilibrium protein concentrations (> ~0.3 (g BSA)/L), likely as a result of Macro-Prep(®) acting as an unrestricted multilayer adsorbent at these conditions. These data can be used to inform the design and scale-up of ion-exchange columns for removing proteins from wines. |
format | Online Article Text |
id | pubmed-8272113 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-82721132021-07-11 Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment Sun, Lin Srinivas, Ananya Runnebaum, Ron C. Molecules Article The impact of key classes of compounds found in wine on protein removal by the ion-exchange resin, Macro-Prep(®) High S, was examined by adsorption isotherm experiments. A model wine system, which contained a prototypical protein Bovine Serum Albumin (BSA), was used. We systematically changed concentrations of individual chemical components to generate and compare adsorption isotherm plots and to quantify adsorption affinity or capacity parameters of Macro-Prep(®) High S ion-exchange resin. The pH (hydronium ion concentration), ethanol concentration, and prototypical phenolics and polysaccharide compounds are known to impact interactions with proteins and thus could alter the adsorption affinity and capacity of Macro-Prep(®) High S ion-exchange resin. At low equilibrium protein concentrations (< ~0.3 (g BSA)/L) and at high equilibrium protein concentrations in model wines at various pH, the adsorption behavior followed the Langmuir isotherm, most likely due to the resin acting as a monolayer adsorbent. The resulting range of BSA capacity was between 0.15–0.18 (g BSA)/(g Macro-Prep(®) High S resin). With the addition of ethanol, catechin, caffeic acid, and polysaccharides, the protein adsorption behavior was observed to differ at higher equilibrium protein concentrations (> ~0.3 (g BSA)/L), likely as a result of Macro-Prep(®) acting as an unrestricted multilayer adsorbent at these conditions. These data can be used to inform the design and scale-up of ion-exchange columns for removing proteins from wines. MDPI 2021-06-26 /pmc/articles/PMC8272113/ /pubmed/34206735 http://dx.doi.org/10.3390/molecules26133905 Text en © 2021 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 Sun, Lin Srinivas, Ananya Runnebaum, Ron C. Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment |
title | Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment |
title_full | Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment |
title_fullStr | Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment |
title_full_unstemmed | Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment |
title_short | Understanding the Impact of Key Wine Components on the Use of a Non-Swelling Ion-Exchange Resin for Wine Protein Fining Treatment |
title_sort | understanding the impact of key wine components on the use of a non-swelling ion-exchange resin for wine protein fining treatment |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8272113/ https://www.ncbi.nlm.nih.gov/pubmed/34206735 http://dx.doi.org/10.3390/molecules26133905 |
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