Evidence map›Paper›PMID 40954166›Full record

ArticleScientific reports2025

Enhancement of antioxidant and antimicrobial properties of Whey protein isolate and chlorogenic acid complexes through enzymatic and alkaline techniques.

Mostafa Ali, Mohamed Yousef, Mahmoud Khalil, Amira Rizk, Yemane H Gebremeskal, Fawaz Alzahrani, Atef Fathy Ahmed, Aml Abubakr Tantawy, Mohamed Said Boulkrane, Denis A Baranenko and 2 more

Abstract read
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Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
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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

12 authors.

Mostafa AliFood Technology Department, Faculty of Agriculture, Kafrelsheikh University, Kafr El-Sheikh, Egypt. mostafa.ali@agr.kfs.edu.eg.
Mohamed YousefFood Technology Department, Faculty of Agriculture, Kafrelsheikh University, Kafr El-Sheikh, Egypt.
Mahmoud KhalilNutritional Science Institute, Potsdam University, Potsdam, Germany.
Amira RizkFood Science and Technology Department, Faculty of Agriculture, Tanta University, Tanta, Egypt.
Yemane H GebremeskalInternational Research Centre "Biotechnologies of the Third Millennium", Faculty of Biotechnologies (BioTech), ITMO University, Saint Petersburg, 91002, Russia.
Fawaz AlzahraniDepartment of Biology, College of Science, Taif University, P.O. Box 11099, Taif, 21944, Saudi Arabia.
Atef Fathy AhmedDepartment of Biology, College of Science, Taif University, P.O. Box 11099, Taif, 21944, Saudi Arabia.
Aml Abubakr TantawyFood Science Department, Faculty of Agriculture, Beni-Suef University, Beni-Suef, 65211, Egypt.
Mohamed Said BoulkraneInternational Research Centre "Biotechnologies of the Third Millennium", Faculty of Biotechnologies (BioTech), ITMO University, Saint Petersburg, 91002, Russia.
Denis A BaranenkoInternational Research Centre "Biotechnologies of the Third Millennium", Faculty of Biotechnologies (BioTech), ITMO University, Saint Petersburg, 91002, Russia.
Tamer M El-MesseryInternational Research Centre "Biotechnologies of the Third Millennium", Faculty of Biotechnologies (BioTech), ITMO University, Saint Petersburg, 91002, Russia.
Samar AlyFood Science and Technology Department, Faculty of Agriculture, Tanta University, Tanta, Egypt.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interactions of whey protein isolate (WPI) with chlorogenic acid (CQA) using two techniques, alkaline (pH 9) and enzymatic (tyrosinase) were investigated. Complexes, formed between WPI and CQA by alkaline technique (AWPI-CQA) and enzymatic technique (EWPI-CQA), compared to control WPI (CWPI), were characterized in terms of their chemical, structural, emulsifying, antioxidant, and antibacterial properties. Compared to CWPI, both complexation methods significantly reduced free amino groups (CWPI: 588.00 nmol/mg; AWPI-CQA: 409.85 nmol/mg; EWPI-CQA: 412.50 nmol/mg), sulfhydryl groups (CWPI: 68.01 nmol/mg; AWPI-CQA: 18.43 nmol/mg; EWPI-CQA: 48.91 nmol/mg), and tryptophan content (CWPI: 61.21 nmol/mg; AWPI-CQA: 30.12 nmol/mg; EWPI-CQA: 37.64 nmol/mg). Changes in protein structure were examined using internal fluorescence spectra, ultraviolet-visible spectra (UV-Vis) scan, and ultrahigh performance liquid chromatography with electrospray ionization and quadrupole time-of-flight mass spectrometry (UHPLC-ESI-Q-TOF-MS). WPI fluorescence spectra showed that CQA leads to quenching of protein fluorescence. ESI-MS data show that one or more CQA molecules are covalently bound to WPI under both conditions. In addition, AWPI-CQA showed high antioxidative capacity compared to EWPI-CQA and CWPI. On the other hand, EWPI-CQA exhibited notable antimicrobial activity against Staphylococcus aureus LMG 10,147 and MU50 in comparison to AWPI-CQA and CWPI. The development of nutraceutical foods meets the modern consumer needs. Therefore, WPI-CQA complexes can be used as functional components in many food products. Moreover, consumers may benefit from the health-enhancing effects of phenolic compounds.

Indexed as

Anti-Bacterial AgentsAnti-Infective AgentsAntioxidantsChlorogenic AcidWhey ProteinsMicrobial Sensitivity TestsStaphylococcus aureusAnti-Bacterial AgentsAnti-Infective AgentsAntioxidantsChlorogenic AcidWhey ProteinsAntibacterial and antioxidant activityChlorogenic acidComplexesWhey protein isolate

Identifiers

PMID40954166
PMCPMC12436586

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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.