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Open AccessArticle

Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins

Dr. von Hauner Children’s Hospital, Ludwig Maximilians University Munich, Lindwurm Str. 4, 80337 Munich, Germany
Comprehensive Pneumology Centre Munich (CPC-M), Member of the German Center of Lung Reseach (DZL), 80337 Munich, Germany
Laboratory of Biochemistry, Wageningen University, 6708 WE Wageningen, The Netherlands
Helmholtz Zentrum München—German Research Center for Environmental Health, Institute for Asthma and Allergy Prevention, Ingolstädter Landstr. 1, 85764 Neuherberg, Germany
Dairy Science and Technology, Food Quality and Design Group, Wageningen University, 6708 PB Wageningen, The Netherlands
Author to whom correspondence should be addressed.
Nutrients 2017, 9(9), 963;
Received: 14 June 2017 / Revised: 23 August 2017 / Accepted: 25 August 2017 / Published: 31 August 2017
(This article belongs to the Special Issue Nutrition and Allergic Diseases)
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. View Full-Text
Keywords: proteomics; heat stability; milk serum proteins; immune-active proteins proteomics; heat stability; milk serum proteins; immune-active proteins
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Brick, T.; Ege, M.; Boeren, S.; Böck, A.; Von Mutius, E.; Vervoort, J.; Hettinga, K. Effect of Processing Intensity on Immunologically Active Bovine Milk Serum Proteins. Nutrients 2017, 9, 963.

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