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Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects

Proteinaceous products are widely used as fining agents during winemaking to remove unwanted insoluble particles and undissolved microscopic particles (colloidal material) from the must or wine to improve stability. Some of them (egg white, caseinates, and fish gelatine) have allergenic potential an...

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Detalles Bibliográficos
Autores principales: Peñas, Elena, di Lorenzo, Chiara, Uberti, Francesca, Restani, Patrizia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6332064/
https://www.ncbi.nlm.nih.gov/pubmed/26197307
http://dx.doi.org/10.3390/molecules200713144
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author Peñas, Elena
di Lorenzo, Chiara
Uberti, Francesca
Restani, Patrizia
author_facet Peñas, Elena
di Lorenzo, Chiara
Uberti, Francesca
Restani, Patrizia
author_sort Peñas, Elena
collection PubMed
description Proteinaceous products are widely used as fining agents during winemaking to remove unwanted insoluble particles and undissolved microscopic particles (colloidal material) from the must or wine to improve stability. Some of them (egg white, caseinates, and fish gelatine) have allergenic potential and the presence of their residues in the final product could represent a risk for allergic individuals. Moreover, lysozyme (an egg allergen) is included among wine additives to control the fermentation processes and avoid spoiling during winemaking. The aim of this paper is to review the experimental/clinical data on the use of allergenic products in enology and the measurement of relative risk for sensitized subjects. In addition, methods developed specifically for the quantification of allergenic residues in must and wine are described.
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spelling pubmed-63320642019-01-24 Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects Peñas, Elena di Lorenzo, Chiara Uberti, Francesca Restani, Patrizia Molecules Review Proteinaceous products are widely used as fining agents during winemaking to remove unwanted insoluble particles and undissolved microscopic particles (colloidal material) from the must or wine to improve stability. Some of them (egg white, caseinates, and fish gelatine) have allergenic potential and the presence of their residues in the final product could represent a risk for allergic individuals. Moreover, lysozyme (an egg allergen) is included among wine additives to control the fermentation processes and avoid spoiling during winemaking. The aim of this paper is to review the experimental/clinical data on the use of allergenic products in enology and the measurement of relative risk for sensitized subjects. In addition, methods developed specifically for the quantification of allergenic residues in must and wine are described. MDPI 2015-07-21 /pmc/articles/PMC6332064/ /pubmed/26197307 http://dx.doi.org/10.3390/molecules200713144 Text en © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Peñas, Elena
di Lorenzo, Chiara
Uberti, Francesca
Restani, Patrizia
Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects
title Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects
title_full Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects
title_fullStr Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects
title_full_unstemmed Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects
title_short Allergenic Proteins in Enology: A Review on Technological Applications and Safety Aspects
title_sort allergenic proteins in enology: a review on technological applications and safety aspects
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6332064/
https://www.ncbi.nlm.nih.gov/pubmed/26197307
http://dx.doi.org/10.3390/molecules200713144
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