Evidence map›Paper›PMID 40242401›Full record

ArticleCurrent research in food science2025

Preparation, structural characterization, and functional properties of a tilapia-soybean dual proteins: Effects of different complexation modes.

Xinyi Qin, Pengzhi Hong, Liangyu Zhao, Mengya Xie, Chunxia Zhou, Qingguan Liu

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Article in Current research in food science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper 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

6 authors.

Xinyi QinCollege of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China.
Pengzhi HongCollege of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China.
Liangyu ZhaoCollege of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China.
Mengya XieCollege of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China.
Chunxia ZhouCollege of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China.
Qingguan LiuCollege of Food Science and Technology, Guangdong Ocean University, Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Marine Food, Guangdong Provincial Modern Agricultural Science and Technology Innovation Center, Zhanjiang, 524088, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The limited functional properties of tilapia protein isolate (TPI), such as low solubility, emulsification, and foaming, restrict its use in the food industry. However, combining it with hydrophilic proteins can improve these properties. Different assembly methods may affect the structure and functionality of the resulting dual proteins. To study this, tilapia-soybean protein mixtures (T-SPM), complexes (T-SPC), and co-precipitates (T-SPCP) were prepared using physical mixing, pH-regulated complexation, and pH-regulated co-precipitation. The effects of these methods on the structure and functional properties of the tilapia-soybean dual proteins were then analyzed. Structural analysis revealed that TPI combined with SPI through non-covalent forces and disulfide bonds under pH-regulation, leading to structural changes. Compared to T-SPCP, T-SPC showed more hydrophilic groups, with increased free sulfhydryl groups, disulfide bonds, α-helices, and zeta potential, alongside reduced surface hydrophobicity and smaller flake structures. Functional analysis indicated that pH-regulated assembly methods significantly improved the properties of the dual proteins compared to T-SPM. T-SPC exhibited higher solubility, emulsification, and foaming capacity than T-SPCP, which had a more aggregated structure due to pH adjustment to 4.5 during co-precipitation, contributing to its better thermal stability. Thus, T-SPC, assembled by pH-regulation from 12.0 to 7.0, demonstrated superior characteristics. This study offers a theoretical foundation for developing functional dual proteins and their food industry applications.

Indexed as

Dual proteinFunctional propertiespH-regulationSoybean protein isolateTilapia protein isolate

Identifiers

PMID40242401
PMCPMC12002791

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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.