Evidence map›Paper›PMID 36193486›Full record

ArticleJournal of food science and technology2022

Improvement of functional properties of cow's milk peptides through partial proteins hydrolysis.

Thais S Milessi, Laiane A Lopes, Paula K Novelli, Paulo W Tardioli, Raquel L C Giordano

Open access · greenAbstract read
In one paragraph

Article in Journal of food science and technology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 45% of its field
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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 1 institution in 1 country.

Thais S MilessiDepartment of Chemical Engineering, Federal University of São Carlos, Rodovia Washington Luíz, km 235, São Carlos, SP 13565-905 Brazil.ORCID 0000-0001-5007-5818
Laiane A LopesGraduate Program of Chemical Engineering, Federal University of São Carlos (PPEQ-UFSCar), Rodovia Washington Luíz, km 235, São Carlos, SP 13565-905 Brazil.
Paula K NovelliDepartment of Chemical Engineering, Federal University of São Carlos, Rodovia Washington Luíz, km 235, São Carlos, SP 13565-905 Brazil.
Paulo W TardioliDepartment of Chemical Engineering, Federal University of São Carlos, Rodovia Washington Luíz, km 235, São Carlos, SP 13565-905 Brazil.
Raquel L C GiordanoDepartment of Chemical Engineering, Federal University of São Carlos, Rodovia Washington Luíz, km 235, São Carlos, SP 13565-905 Brazil.
Universidade Federal de São Carlos · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allergy by cow's milk proteins is among the major food allergies and could be reduced by the partial hydrolysis of these proteins by proteases, without significantly affecting its physicochemical properties. In addition, the peptides generated through enzymatic hydrolysis of the cow's milk can present prebiotic and bioactive properties. In this work, the cow's milk proteins were submitted to a controlled hydrolysis by Novo-Pro D® and the influence of the degree of hydrolysis (DH) on peptide size distribution was evaluated, as well as the prebiotic and antimicrobial properties of milk hydrolysates. It was shown that for DH-10%, all the peptides have sizes lower than 12 kDa which is the size of the most allergenic proteins, without apparent changes in the milk, as long as heating of the hydrolysate is avoided. The protein hydrolysis promoted a great improvement in the milk functional properties. In addition, the obtained milk peptides presented great prebiotic activities, as indicated by the significant improvement of the growth of prebiotic Supplementary Information: The online version contains supplementary material available at 10.1007/s13197-022-05533-x.

Indexed as

Antimicrobial activityEnzymatic proteolysisMilk peptidesMultifunctional propertiesPrebiotics

Identifiers

PMID36193486
PMCPMC9525475
OpenAlexW4283461217

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.