Evidence map›Paper›PMID 28858242›Full record

ArticleNutrients2017

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

Abstract read
In one paragraph

Article in Nutrients, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

  1. Trial
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  17. Milk processing increases the allergenicity of cow's milk-Preclinical evidence supported by a human proof-of-concept provocation pilot.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Tabea BrickDr. von Hauner Children's Hospital, Ludwig Maximilians University Munich, Lindwurm Str. 4, 80337 Munich, Germany. tabea.brick@med.uni-muenchen.de.
Markus EgeDr. von Hauner Children's Hospital, Ludwig Maximilians University Munich, Lindwurm Str. 4, 80337 Munich, Germany. Markus.Ege@med.uni-muenchen.de.
Sjef BoerenLaboratory of Biochemistry, Wageningen University, 6708 WE Wageningen, The Netherlands. sjef.boeren@wur.nl.
Andreas BöckDr. von Hauner Children's Hospital, Ludwig Maximilians University Munich, Lindwurm Str. 4, 80337 Munich, Germany. A.Boeck@med.uni-muenchen.de.
Erika von MutiusDr. von Hauner Children's Hospital, Ludwig Maximilians University Munich, Lindwurm Str. 4, 80337 Munich, Germany. Erika.Von.Mutius@med.uni-muenchen.de.
Jacques VervoortLaboratory of Biochemistry, Wageningen University, 6708 WE Wageningen, The Netherlands. jacques.vervoort@wur.nl.
Kasper HettingaDairy Science and Technology, Food Quality and Design Group, Wageningen University, 6708 PB Wageningen, The Netherlands. kasper.hettinga@wur.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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,

Indexed as

AnimalsCattleFood HandlingHot TemperatureMilkMilk ProteinsPasteurizationMilk Proteinsheat stabilityimmune-active proteinsmilk serum proteinsproteomics

Identifiers

PMID28858242
PMCPMC5622723

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.