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An Effective Method of Isolating Honey Proteins

Honey is a natural sweetener composed mostly of sugars, but it contains also pollen grains, proteins, free amino acids, and minerals. The amounts and proportions of these components depend on the honey type and bee species. Despite the low content of honey protein, they are becoming a popular study...

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Detalles Bibliográficos
Autores principales: Bocian, Aleksandra, Buczkowicz, Justyna, Jaromin, Marcin, Hus, Konrad Kamil, Legáth, Jaroslav
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6651845/
https://www.ncbi.nlm.nih.gov/pubmed/31261846
http://dx.doi.org/10.3390/molecules24132399
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author Bocian, Aleksandra
Buczkowicz, Justyna
Jaromin, Marcin
Hus, Konrad Kamil
Legáth, Jaroslav
author_facet Bocian, Aleksandra
Buczkowicz, Justyna
Jaromin, Marcin
Hus, Konrad Kamil
Legáth, Jaroslav
author_sort Bocian, Aleksandra
collection PubMed
description Honey is a natural sweetener composed mostly of sugars, but it contains also pollen grains, proteins, free amino acids, and minerals. The amounts and proportions of these components depend on the honey type and bee species. Despite the low content of honey protein, they are becoming a popular study object, and have recently been used as markers of the authenticity and quality of honey. Currently, the most popular methods of protein isolation from honey are dialysis against distilled water, lyophilization of dialysate, or various precipitation protocols. In this work, we propose a new method based on saturated phenol. We tested it on three popular polish honey types and we proved its compatibility with both 1D and 2D polyacrylamide gel electrophoresis (PAGE) and MS (mass spectrometry) techniques. The elaborated technique is also potentially less expensive and less time-consuming than other previously described methods, while being equally effective.
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spelling pubmed-66518452019-08-08 An Effective Method of Isolating Honey Proteins Bocian, Aleksandra Buczkowicz, Justyna Jaromin, Marcin Hus, Konrad Kamil Legáth, Jaroslav Molecules Article Honey is a natural sweetener composed mostly of sugars, but it contains also pollen grains, proteins, free amino acids, and minerals. The amounts and proportions of these components depend on the honey type and bee species. Despite the low content of honey protein, they are becoming a popular study object, and have recently been used as markers of the authenticity and quality of honey. Currently, the most popular methods of protein isolation from honey are dialysis against distilled water, lyophilization of dialysate, or various precipitation protocols. In this work, we propose a new method based on saturated phenol. We tested it on three popular polish honey types and we proved its compatibility with both 1D and 2D polyacrylamide gel electrophoresis (PAGE) and MS (mass spectrometry) techniques. The elaborated technique is also potentially less expensive and less time-consuming than other previously described methods, while being equally effective. MDPI 2019-06-29 /pmc/articles/PMC6651845/ /pubmed/31261846 http://dx.doi.org/10.3390/molecules24132399 Text en © 2019 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 (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Bocian, Aleksandra
Buczkowicz, Justyna
Jaromin, Marcin
Hus, Konrad Kamil
Legáth, Jaroslav
An Effective Method of Isolating Honey Proteins
title An Effective Method of Isolating Honey Proteins
title_full An Effective Method of Isolating Honey Proteins
title_fullStr An Effective Method of Isolating Honey Proteins
title_full_unstemmed An Effective Method of Isolating Honey Proteins
title_short An Effective Method of Isolating Honey Proteins
title_sort effective method of isolating honey proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6651845/
https://www.ncbi.nlm.nih.gov/pubmed/31261846
http://dx.doi.org/10.3390/molecules24132399
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