Effect of processing intensity on immunologically active bovine milk serum proteins

Tabea Brick, Markus Ege*, Sjef Boeren, Andreas Böck, Erika Von Mutius, Jacques Vervoort, Kasper Hettinga

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

13 Citations (Scopus)

Abstract

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.
Original languageEnglish
Article number963
Pages (from-to)1-14
JournalNutrients
Volume9
Issue number9
DOIs
Publication statusPublished - 2017

Fingerprint

Milk Proteins
whey
blood proteins
Blood Proteins
Milk
raw milk
heat
Hot Temperature
milk
asthma
heat treatment
processing technology
boiling
hypersensitivity
lactadherin
shelf life
proteins
lactoferrin
milk proteins
Respiratory Tract Infections

Keywords

  • Heat stability
  • Immune-active proteins
  • Milk serum proteins
  • Proteomics

Cite this

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. In: Nutrients. 2017 ; Vol. 9, No. 9. pp. 1-14.
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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.

In: Nutrients, Vol. 9, No. 9, 963, 2017, p. 1-14.

Research output: Contribution to journalArticleAcademicpeer-review

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T1 - Effect of processing intensity on immunologically active bovine milk serum proteins

AU - Brick, Tabea

AU - Ege, Markus

AU - Boeren, Sjef

AU - Böck, Andreas

AU - Von Mutius, Erika

AU - Vervoort, Jacques

AU - Hettinga, Kasper

PY - 2017

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N2 - 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.

AB - 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.

KW - Heat stability

KW - Immune-active proteins

KW - Milk serum proteins

KW - Proteomics

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SN - 2072-6643

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M1 - 963

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