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Effects of transglutaminase pre-crosslinking on salt-induced gelation of soy protein isolate emulsion
Open accessAbstract
The salt-induced gelation behavior of soy protein isolate (SPI) emulsions was markedly influenced by microbial transglutaminase (TGase) pre-crosslinking. Rheological data showed that when SPI emulsions were incubated with TGase at low concentrations (1 and 3 U/g protein) at 50 °C for 30 min prior to gelation, no change in storage modulus (G′), but enhanced resistance to deformation of the gels was observed. Extensive crosslinking by TGase (5 U/g protein) resulted in severe decreases in gel firmness and fracture properties (yielding stress and strain), likely due to the impairment of hydrophobic bonds and the formation of coarse networks. The water-holding capacity of the gels was significantly enhanced by increased concentrations of TGase. Interactive force analysis indicated that non-covalent interactions and disulfide bonds are the primary forces involved in CaSO4-induced SPI emulsion gel, but TGase treatment may limit hydrophobic interactions within the gel network. These results are of great potential value for the application of TGase in the food industry.
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Low concentrations of transglutaminase (1 and 3 U/g) significantly improved the gel structure and resistance to deformation of salt-induced soy protein isolate gels.
“Luo et al. (2019) explored the impact of TGase precrosslinking on salt-induced gelation of SPI and found that low concentrations of TGase (1 and 3 U/g) significantly improved the gel structure and resistance to deformation.”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Luo et al. (2019)
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Cited by
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Li, B., Luan, H., Qin, J., Zong, A., Liu, L., Xu, Z., Du, F., & Xu, T. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129806 · Cited by 41
A Review of Gelation of Plant Proteins and Their Influencing Factors
Hui, D., Liang, W., Wang, R., Feng, X., & Tang, X. (2025) · Sustainable Food Proteins · doi:10.1002/sfp2.70037 · Cited by 12
Metadata
- Authors
- Luo, K., Liu, S., Miao, S., Adhikari, B., Wang, X., & Chen, J.
- Affiliations
- Jiangnan University (CN)
- Fuzhou University (CN)
- Teagasc - The Irish Agriculture and Food Development Authority (IE)
- RMIT University (AU)
- Corresponding author
- Wang, Xufeng
- Chen, Jie
- Venue
- Journal of Food Engineering
- Publisher
- Elsevier BV
- Published
- 2019-12
- Volume
- 263
- Pages
- 280-287
- ISSN
- 0260-8774 (ISSN-L)
- OpenAlex
- W2957775694
- Cited by
- 88
- References
- 0
- Citations by year
- 2026: 13 · 2025: 12 · 2024: 13 · 2023: 16 · 2022: 13 · 2021: 11 · 2020: 9 · 2019: 1
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Journal of Food Engineering (publishedVersion)
- T-Stór (Teagasc) (acceptedVersion, cc-by-nc-sa)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion, cc-by-nc-sa)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- Figshare (submittedVersion)
- Funders
- National High-tech Research and Development Program
- National Natural Science Foundation of China
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Keywords
- soy protein isolate, emulsion gelation, salt-induced gelation, microbial transglutaminase, pre-crosslinking, calcium sulfate, gel strength, fracture behavior, water holding capacity, hydrophobic interactions, disulfide bonds, non-covalent interactions, gel network structure, rheological properties
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