Assessing the Functional and Structural Properties of Peanut Meals Modified by Transglutaminase-Coupled Glycation.

Yan Liu, Tingwei Zhu, Fusheng Chen, Xingfeng Guo, Chenxian Yang, Yu Chen, Lifen Zhang

Abstract read

In one paragraph

Article in Foods (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

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

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

1 citing paper in PubMed.

Structural Modification and Enhanced Gel Properties of Peanut Protein via Co-Precipitation with Egg White Protein.Foods (Basel, Switzerland) · 2026
Article

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

7 authors.

Yan LiuCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Tingwei ZhuCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.ORCID 0000-0001-6807-0900

Fusheng ChenCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Xingfeng GuoCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Chenxian YangCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Yu ChenCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Lifen ZhangCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, China.

Funding

the Collaboration Project with Yihai Kerry (Qingdao) Flavor Food Application Innovation Center Co., Ltd E-202109-03874-QRthe Cultivation Project of Tuoxin Team in Henan University of Technology 2024TXTD04the National Key R＆D Program of China 2023YFD2100402the Science and Technology Project of Henan Province 242102110096the Science and Technology Project of Henan Province 252102110089the Young Elite Scientists Sponsorship Program by Henan Association for Science and Technology 2025HYTP057

6 · The paper itself

Abstract

To increase the added value of peanut meal (PM, protein content of 46.17%) and expand its application in food processing, cold-pressed PM was modified via transglutaminase (TGase)-coupled glycation to enhance its functional properties. The effects of the modification conditions (i.e., PM concentration, PM/glucose mass ratio, temperature, and time) on the functional properties of PM were investigated, and its structural properties were evaluated using water contact angle measurements, fluorescence spectroscopy, and Fourier-transform infrared spectroscopy. It was found that TGase-coupled glycation modification altered the secondary structure of PM and increased both the water contact angle and the surface hydrophobicity, thereby significantly affecting its functional properties. Additionally, superior emulsification, foaming, and oil-absorbing properties were achieved for the modified PM, which were named EPM, FPM, and OPM, respectively (specimens under different modification conditions). Notably, the emulsification activity of the EPM sample was enhanced by 69.8% (i.e., from 18.48 to 31.38 m

Indexed as

functional propertiesglycationpeanut mealstructuretransglutaminase

Identifiers

PMID40509526

DOI10.3390/foods14111999

PMCPMC12154547

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.