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Microbial transglutaminase promotes cross-linking for enhancing gelation of myofibrillar protein in frozen Litopenaeus vannamei through deamination reaction
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“excessive TG destroyed the stable gel structure, exposing more digestive sites to enzymes and consequently promoting proteolysis”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Z. Chen, Dai, et al. 2024
In the citing paper
“This phenomenon is presumably associated with TG‐mediated crosslinking along with raised disulfide bonds in protein gels, which potentially reduces the exposure of digestion sites and restricts the diffusivity and accessibility of enzymes.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Z. Chen, Dai, et al. 2024
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“Moderate addition of TG could enhance mechanical properties of protein gels, such as increased gel strength and denser microstructure, ultimately reducing proteolysis.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Z. Chen, Dai, et al. 2024
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“Shrimp surimi products are highly favored by consumers worldwide due to their high protein and low fat nutritional profiles, coupled with their unique elastic texture (Chen et al., 2024; Walayat et al., 2025).”
Zhang, X., Wu, S., Tang, C., Yang, Z., Wang, W. C., Xu, Y., Li, C., Zhou, H. J., & Xu, B. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153713
Wang, K., Jia, Y., Ren, Y.-Y., Zhang, Y., Yu, C., Lu, F., & Liu, Y.-H. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113116
Yuan, D., Liu, Y., Li, C., Kong, B., Cao, C., Zhang, H., Zhang, H., Liu, Q., & Feng, Y. (2026) · Meat Science · doi:10.1016/j.meatsci.2026.110165
Zhang, Y.-J., Rahman, Z., Song, H.-W., Xiong, S.-B., Yin, T., Liu, R., & You, J. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149432
Yin, Y., Liu, Y., Lu, J.-Q., Lu, Y., Yin, C.-X., Cai, J., Guo, T., Liu, Y., Wei, S., Cao, Y.-Q., et al. (2026) · The Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.70614
“10 This crosslinking strengthens the gel network, improving gel strength, elasticity, and WHC. 1 However, the solo application of TG also has drawbacks: excessive addition can lead to over-crosslinking, causing a decrease in the digestibility of protein.”
Varsha, D., Balange, A. K., Layana, P., Deepitha, R., Iburahim, D. A., Joshi, S. A., & Gore, S. B. (2025) · International Journal of Bio-resource and Stress Management · doi:10.23910/1.2025.5979
“…transglutaminase treatment alters the secondary structure, cross-linking, and aggregation of shrimp myofibrillar protein through deamination, enhancing gel properties by catalyzing γ -carboxyl and ε -amino group reactions, increasing disulfide bonds, and improving gel strength (Chen et al., 2024).”
Determined Transglutaminase 1 Activity in Blood Serum for Brain Cancer Patients and Healthy People
Ibrahim, A., & Rashed, S. (2024) · South Eastern European Journal of Public Health · doi:10.70135/seejph.vi.1476
“According to a study, transglutaminases may contribute to the development of cancer, especially brain tumors (BT) [10].”
BackgroundZhang, Y., Jia, Y., He, X., Sun, G., Wang, K., Liu, Y., Lu, F., & Liu, Y. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112773
Zaghbib, I., Harrazi, N., Hassouna, M., Salmi, C., Mohammed, H. A., Bouafia, A., Laouini, S. E., & Abdullah, J. (2026) · Sustainable Food Technology · doi:10.1039/d6fb00112b
Metadata
- Authors
- Chen, Z., Dai, Z., Liu, C., Wang, S., Li, J., & Mao, X.
- Affiliations
- Ocean University of China (CN)
- Qingdao National Laboratory for Marine Science and Technology (CN)
- Corresponding author
- Li, Jiao
- Mao, Xiangzhao
- Venue
- Food Hydrocolloids
- Publisher
- Elsevier BV
- Published
- 2024-02
- Volume
- 147
- Pages
- 109332
- ISSN
- 0268-005X (ISSN-L)
- OpenAlex
- W4386984081
- Cited by
- 48
- References
- 0
- Citations by year
- 2026: 14 · 2025: 15 · 2024: 19
- FWCI
- 8.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Hydrocolloids (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- microbial transglutaminase, crosslinking, myofibrillar proteins, frozen shrimp, Litopenaeus vannamei, gelation, deamination, protein secondary structure, disulfide bonds, water holding capacity, gel strength, protein network structure, pepsin hydrolysis, free amino groups
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