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Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins

Consumption of raw cow’s milk instead of industrially processed milk has been reported to protect children from developing asthma, allergies, and respiratory infections. Several heat-sensitive milk serum proteins have been implied in this effect though unbiased assessment of milk proteins in general...

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Autores principales: Brick, Tabea, Ege, Markus, Boeren, Sjef, Böck, Andreas, von Mutius, Erika, Vervoort, Jacques, Hettinga, Kasper
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5622723/
https://www.ncbi.nlm.nih.gov/pubmed/28858242
http://dx.doi.org/10.3390/nu9090963
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author Brick, Tabea
Ege, Markus
Boeren, Sjef
Böck, Andreas
von Mutius, Erika
Vervoort, Jacques
Hettinga, Kasper
author_facet Brick, Tabea
Ege, Markus
Boeren, Sjef
Böck, Andreas
von Mutius, Erika
Vervoort, Jacques
Hettinga, Kasper
author_sort Brick, Tabea
collection PubMed
description Consumption of raw cow’s milk instead of industrially processed milk has been reported to protect children from developing asthma, allergies, and respiratory infections. Several heat-sensitive milk serum proteins have been implied in this effect though unbiased assessment of milk proteins in general is missing. The aim of this study was to compare the native milk serum proteome between raw cow’s milk and various industrially applied processing methods, i.e., homogenization, fat separation, pasteurization, ultra-heat treatment (UHT), treatment for extended shelf-life (ESL), and conventional boiling. Each processing method was applied to the same three pools of raw milk. Levels of detectable proteins were quantified by liquid chromatography/tandem mass spectrometry following filter aided sample preparation. In total, 364 milk serum proteins were identified. The 140 proteins detectable in 66% of all samples were entered in a hierarchical cluster analysis. The resulting proteomics pattern separated mainly as high (boiling, UHT, ESL) versus no/low heat treatment (raw, skimmed, pasteurized). Comparing these two groups revealed 23 individual proteins significantly reduced by heating, e.g., lactoferrin (log2-fold change = −0.37, p = 0.004), lactoperoxidase (log2-fold change = −0.33, p = 0.001), and lactadherin (log2-fold change = −0.22, p = 0.020). The abundance of these heat sensitive proteins found in higher quantity in native cow’s milk compared to heat treated milk, renders them potential candidates for protection from asthma, allergies, and respiratory infections.
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spelling pubmed-56227232017-10-05 Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins Brick, Tabea Ege, Markus Boeren, Sjef Böck, Andreas von Mutius, Erika Vervoort, Jacques Hettinga, Kasper Nutrients Article Consumption of raw cow’s milk instead of industrially processed milk has been reported to protect children from developing asthma, allergies, and respiratory infections. Several heat-sensitive milk serum proteins have been implied in this effect though unbiased assessment of milk proteins in general is missing. The aim of this study was to compare the native milk serum proteome between raw cow’s milk and various industrially applied processing methods, i.e., homogenization, fat separation, pasteurization, ultra-heat treatment (UHT), treatment for extended shelf-life (ESL), and conventional boiling. Each processing method was applied to the same three pools of raw milk. Levels of detectable proteins were quantified by liquid chromatography/tandem mass spectrometry following filter aided sample preparation. In total, 364 milk serum proteins were identified. The 140 proteins detectable in 66% of all samples were entered in a hierarchical cluster analysis. The resulting proteomics pattern separated mainly as high (boiling, UHT, ESL) versus no/low heat treatment (raw, skimmed, pasteurized). Comparing these two groups revealed 23 individual proteins significantly reduced by heating, e.g., lactoferrin (log2-fold change = −0.37, p = 0.004), lactoperoxidase (log2-fold change = −0.33, p = 0.001), and lactadherin (log2-fold change = −0.22, p = 0.020). The abundance of these heat sensitive proteins found in higher quantity in native cow’s milk compared to heat treated milk, renders them potential candidates for protection from asthma, allergies, and respiratory infections. MDPI 2017-08-31 /pmc/articles/PMC5622723/ /pubmed/28858242 http://dx.doi.org/10.3390/nu9090963 Text en © 2017 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
Brick, Tabea
Ege, Markus
Boeren, Sjef
Böck, Andreas
von Mutius, Erika
Vervoort, Jacques
Hettinga, Kasper
Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins
title Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins
title_full Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins
title_fullStr Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins
title_full_unstemmed Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins
title_short Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins
title_sort effect of processing intensity on immunologically active bovine milk serum proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5622723/
https://www.ncbi.nlm.nih.gov/pubmed/28858242
http://dx.doi.org/10.3390/nu9090963
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