The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Enzymolysis and homogenization of soybean protein isolate: Structure and gel properties
Abstract
The objective of this study was to enhance the gel properties of soybean protein isolate (SPI), which frequently shows heterogeneous qualities and limited functionality in cold-induced Chiba tofu. In the context of practical production conditions, the impact of limited enzymolysis (0.5% hydrolysis) in conjunction with different homogenization pressures (4-14 MPa) on the structural characteristics and gel properties of SPI was determined. The enzymolysis-homogenization combined treatment (E-HCT) showed a significant enhancement in water holding capacity (WHC), hardness, chewiness, springiness and cohesiveness of the gels in comparison to the control group (P < 0.05). At 10 MPa homogenization pressure, the treatment outcome of the papain-homogenization combined treatment (P-HCT) showed better efficacy in comparison to that of the alkaline protease-homogenization combined treatment (AP-HCT): Its WHC reached 90.80% and hardness was 11.26 ± 0.04 Pa, which was 3.08 times higher than the control group. The analysis of intermolecular forces indicated that non-disulfide covalent bonds, hydrophobic interactions, and disulfide bonds were primarily responsible for stabilizing the gel network. Structural characterization using Raman and Fourier transform infrared spectroscopy (FTIR) spectroscopy showed an increase in α-helix and β-sheet content, accompanied by a decrease in β-turn and random-coil. Scanning electron microscopy (SEM) further showed that E-HCT led to a more uniform, smooth,…
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“Teng et al. demonstrated that protein unfolding facilitates the exposure of previously buried hydrophobic residues and sulfhydryl groups.”
From Heat-induced gelation of ultrasonically extracted saline-alkali-grown soybean protein: Correlation between protein conformation and gel functional behavior (2027) · cites this paper as Teng et al., 2026
In the citing paper
“The increased availability of these reactive sites strengthens hydrophobic association and promotes the formation of disulfide linkages, thereby contributing to a more organized and densely cross-linked gel network (Teng et al., 2026).”
From Heat-induced gelation of ultrasonically extracted saline-alkali-grown soybean protein: Correlation between protein conformation and gel functional behavior (2027) · cites this paper as Teng et al., 2026
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Research works printed but not linked: 5
- Hu, 2023, Influence of heat treatment before and/or after high-pressure homogenization on the structure and emulsification properties of soybean protein isolate, International Journal of Biological Macromolecules, 253
- Lan, 2024, Fabrication of soy protein nanoparticles based on metal-phenolic networks for stabilization of nano-emulsions delivery system, Food Chemistry, 448, 139164, 10.1016/j.foodchem.2024.139164 · DOI
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Han, X., Shan, B., Li, Y., Liu, J., Yang, J., & Li, D. (2027) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.113483
Metadata
- Authors
- Teng, H., Fan, Z., Wang, D., Dong, J., Qian, W., Xing, Y., San, Y., Zheng, L., Wang, Z., Li, B., & Regenstein, J. M.
- Affiliations
- Northeast Agricultural University (CN)
- Cornell University (US)
- Corresponding author
- Zheng, Li
- Li, Bailiang
- Venue
- Food Research International
- Publisher
- Elsevier BV
- Published
- 2026-07
- Volume
- 235
- Pages
- 119150
- ISSN
- 0963-9969 (ISSN-L)
- OpenAlex
- W7154493620
- Cited by
- 1
- References
- 68
- Citations by year
- 2026: 1
- FWCI
- 2.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Research International (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Key Research and Development Program of China (2023YFF1104302)
- Northeast Agricultural University
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- soy protein isolate, enzymolysis, homogenization, gel properties, water holding capacity, gel microstructure, protein secondary structure, papain, alkaline protease, proteolysis
- MeSH terms
- Food Handling, Gels, Hardness, Hydrolysis, Papain, Glycine max, Water, Soybean Proteins, Hydrophobic and Hydrophilic Interactions
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