Evidence map›Paper›PMID 39877688›Full record

ArticleFood chemistry: X2025

Exploring the noncovalent interaction between β-lactoglobulin and flavonoids under nonthermal process: Characterization, physicochemical properties, and potential for lycopene delivering.

Gongshuai Song, Fang Li, Ziming Xu, Nengliang Jiang, Danli Wang, Tinglan Yuan, Ling Li, Jinyan Gong

Abstract read
In one paragraph

Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

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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

8 authors.

Gongshuai SongZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Fang LiZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Ziming XuZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Nengliang JiangZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Danli WangZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Tinglan YuanZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Ling LiZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.
Jinyan GongZhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The poor structure stability and low bioavailability of lycopene (LY) hampers the wide application in food field. Thus, it is crucial to explore novel deliver carrier for LY based on protein-flavonoid complexes. In this study, the noncovalent interaction mechanism between β-lactoglobulin (β-LG) and flavonoids (apigenin (API), luteolin (LUT), myricetin (MY), apigenin-7-O-glucoside, luteolin-7-O-glucoside, and myricetrin) under ultrasound treatment was explored. Results revealed that ultrasound treatment promoted reactive groups exposure and structural unfolding of β-LG to interact with six flavonoids. The main driving force between β-LG and flavonoids was hydrophobic interaction. The docking result showed that the preferred binding site for these flavonoids was on the outer surface of β-LG. The thermal stability, surface hydrophilicity, and antioxidant properties of β-LG-API, β-LG-LUT, and β-LG-MY complexes were superior by multi-spectroscopy methods and molecular simulation analysis (

Indexed as

FlavonoidsLycopeneNoncovalent interactionUltrasoundβ-Lactoglobulin

Identifiers

PMID39877688
PMCPMC11773077

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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.