Evidence map›Paper›PMID 38834001›Full record

ArticleUltrasonics sonochemistry2024

Ultrasound-assisted modification of soybean protein isolate with L-histidine: Relationship between structure and function.

Jingwen Xu, Shizhang Yan, Jing Xu, Baokun Qi

Abstract read
In one paragraph

Article in Ultrasonics sonochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 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

4 authors.

Jingwen XuCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Shizhang YanCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Jing XuCollege of Arts and Sciences, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: xujing@neau.edu.cn.
Baokun QiCollege of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: qibaokun22@163.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herein, the effects of ultrasound-assisted L-histidine (L-His) on the physicochemical properties and conformation of soybean protein isolate (SPI) were investigated. Particle size, zeta potential, turbidity, and solubility were used to evaluate protein aggregation, and the relationship between structural and functional changes of the proteins was characterized using spectral analysis, surface hydrophobicity, emulsification, and antioxidant properties. After ultrasound-assisted L-His treatment, SPI exhibited a smaller particle size, higher solubility, and more homogeneous micromorphology owing to the decrease in alpha-helix content and subsequent increases in zeta potential and active sulfhydryl content. In addition, spectral analysis showed that L-His and SPI could form a complex, which changed the microenvironment of the amino acid residues in SPI, thus improving its emulsification and antioxidant properties. At the concentration of L-His was 0.3 % w/w, the nanocomplex had a smaller particle size (140.03 nm), higher ζ-potential (-23.63 mV), and higher emulsification stability (22.48 min).

Indexed as

AntioxidantsHistidineParticle SizeSoybean ProteinsHydrophobic and Hydrophilic InteractionsSolubilityStructure-Activity RelationshipUltrasonic WavesAntioxidantsHistidineSoybean ProteinsFunctional propertiesL-histidine, UltrasoundSoybean protein isolateStructural characterization

Identifiers

PMID38834001
PMCPMC11179065

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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.