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Riboflavin-loaded soy protein isolate cold gel treated with combination of high intensity ultrasound and high hydrostatic pressure: Gel structure, physicochemical properties and gastrointestinal digestion fate
Open accessAbstract
Transglutaminase (TGase) was added to soy protein isolate (SPI) dispersion after the combination treatment of high intensity ultrasound (HIU) and high hydrostatic pressure (HHP) to catalyze the formation of cold gel, which was used to encapsulate riboflavin. The structure, physicochemical properties and in vitro digestion characteristics of riboflavin-loaded SPI cold gel were investigated. HIU-HHP combined treatment enhanced the strength, water retention, elastic property, thermal stability and protein denaturation degree of riboflavin-loaded SPI cold gels, and improved the gel network structure, resulting in a higher encapsulation efficiency of riboflavin and its chemical stability under heat and light treatment. HIU-HHP combined treatment reduced the erosion and swelling of SPI cold gel in simulated gastrointestinal fluid, and improved the sustained release effect of SPI gel on riboflavin by changing the digestion mode and rate of gel. In addition, HIU-HHP combined treated gels promoted the directional release of riboflavin in the simulated intestinal fluid, thereby improving its bioaccessibility, which was related to the secondary structure orderliness, tertiary conformation tightness and aggregation degree of protein during the gastrointestinal digestion. Therefore, HIU-HHP combined treatment technology had potential application value in improving the protection, sustained/controlled release and delivery of SPI cold gels for sensitive bioactive compounds.
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Over-processing conditions (e.g., prolonged treatment duration or excessively high frequency) may disrupt the gel matrix, thereby increasing the accessibility of enzymes to the protein gel matrix.
“over‐processing conditions (e.g., prolonged treatment duration or excessively high frequency) may disrupt the gel matrix, thereby increasing the accessibility of enzymes to the protein gel matrix”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Mao et al. 2024
The Results and discussion section on protein digestibility says a stable, compact gel network hinders digestive-enzyme permeation, supporting the link between gel structure and enzyme access. But the paper does not report that prolonged processing or excessively high frequency disrupts the matrix; its tested treatments instead strengthened the gel network and reduced digestibility. No page number is available in our copy. (LLM, conf=0.83)
Experimental — accuracy not yet measuredThis structural modification from ultrasound contributes to increased mechanical strength of protein gels, which in turn impairs digestive enzyme activity and reduces digestibility.
“This structural modification contributes to increased mechanical strength of protein gels, which in turn impairs digestive enzyme activity and reduces digestibility.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Mao et al. 2024
The Results and discussion section (“Protein digestibility of gel during gastrointestinal continuous digestion”; page unavailable) reports that ultrasound-treated gels had lower digestibility and suggests that a more compact network hindered digestive enzymes from entering the gel. It does not show that the treatment impaired the enzymes’ activity; the proposed mechanism is reduced access to the protein, not reduced enzyme activity. (LLM, conf=0.88)
Experimental — accuracy not yet measuredUnder optimal processing conditions, ultrasound treatment can unfold protein molecular structures, exposing internal functional groups that enhance molecular interactions among components.
“Under optimal processing conditions, ultrasound treatment can unfold the protein molecular structures, exposing internal functional groups that enhance molecular interactions among components.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Mao et al. 2024
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Metadata
- Authors
- Mao, Y., Li, X., Qi, Q., Wang, F., Zhang, H., Wu, Y., Liu, J., Zhao, C., & Xu, X.
- Affiliations
- Jilin Agricultural University (CN)
- Corresponding author
- Zhao, Chengbin
- Xu, Xiuying
- Venue
- Ultrasonics Sonochemistry
- Publisher
- Elsevier BV
- Published
- 2024-03
- Volume
- 104
- Pages
- 106819
- ISSN
- 1350-4177 (ISSN-L)
- PMC
- PMC10901135
- OpenAlex
- W4391957943
- Cited by
- 29
- References
- 49
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 7
- FWCI
- 6.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Ultrasonics Sonochemistry (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agriculture Research System of China
- National Modern Agriculture Industry Technology System (CARS-02)
- Natural Science Foundation of Jilin Province (20220101347JC)
- National Natural Science Foundation of China (32072217)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Microencapsulation and Drying Processes
- Physical Sciences › Materials Science › Biomaterials › Hydrogels: synthesis, properties, applications
- Keywords
- soy protein isolate, high-intensity ultrasound, high hydrostatic pressure, transglutaminase, gel network structure, encapsulation efficiency, in vitro digestion, sustained drug release, bioaccessibility, bioactive compound delivery, protein secondary and tertiary structure
- MeSH terms
- Digestion, Gels, Hot Temperature, Hydrostatic Pressure, Soybean Proteins
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