Study on the allergenicity and gel properties of transglutaminase cross-linked shrimp myofibrillar protein

This study aims to investigate the allergenicity and gel properties of shrimp myofibrillar protein (MP) cross-linked by different concentrations of transglutaminase (TG) for shrimp gel products. The structural changes of the samples were analyzed using methods such as SDS-PAGE, CD, and UV, revealing that TG cross-linking significantly altered the protein structure. Changes in allergenicity were verified through Western blot and ELISA. The results indicated that TG cross-linked MP reduced its IgE-binding capacity, with the most significant reduction in allergenicity observed at a TG concentration of 90 U/g. The microscopic structure of the gels was validated using 3D printing and scanning electron microscopy, showing significant differences in the aggregation of MP molecules under different concentrations of TG. At 90 U/g, the samples exhibited a tightly knit three-dimensional gel network structure with good printing suitability and precision. This study provides theoretical guidance for producing safer shrimp gel products in the food industry.

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Publication Details

Journal
Food Chemistry
Published
2025-05-24
DOI
https://doi.org/10.1016/j.foodchem.2025.144910
Citations
3
Primary Topic
Proteins in Food Systems
Type
article
Field-Weighted Citation Impact
3.49

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article

Study on the allergenicity and gel properties of transglutaminase cross-linked shrimp myofibrillar protein

Fengju Song, Lu Liu, Lulu Li, Qingli Yang et al.
3 citations
Food Chemistry
Proteins in Food Systems
3.49
article

Study on the allergenicity and gel properties of transglutaminase cross-linked shrimp myofibrillar protein

Fengju Song, Lu Liu, Lulu Li, Qingli Yang, Qingping Gu, Tianjiao Xu, Liangtao Lv
article en
3 citations

Abstract

This study aims to investigate the allergenicity and gel properties of shrimp myofibrillar protein (MP) cross-linked by different concentrations of transglutaminase (TG) for shrimp gel products. The structural changes of the samples were analyzed using methods such as SDS-PAGE, CD, and UV, revealing that TG cross-linking significantly altered the protein structure. Changes in allergenicity were verified through Western blot and ELISA. The results indicated that TG cross-linked MP reduced its IgE-binding capacity, with the most significant reduction in allergenicity observed at a TG concentration of 90 U/g. The microscopic structure of the gels was validated using 3D printing and scanning electron microscopy, showing significant differences in the aggregation of MP molecules under different concentrations of TG. At 90 U/g, the samples exhibited a tightly knit three-dimensional gel network structure with good printing suitability and precision. This study provides theoretical guidance for producing safer shrimp gel products in the food industry.

Food ChemistryVol. 488
Qingdao Agricultural University (CN)
Qingdao Agricultural University, National Natural Science Foundation of China, Natural Science Foundation of Shandong Province
Openalex Percentile: Top 8%
Proteins in Food Systems
3.49
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Study on the allergenicity and gel properties of transglutaminase cross-linked shrimp myofibrillar protein — Fengju Song, Lu Liu, et al. · Food Chemistry (2025) | TGRS Research Map | TGRS