The effect of sweet tea polysaccharide on the physicochemical and structural properties of whey protein isolate gels
Abstract
In this study, we investigated the effect of sweet tea polysaccharide (STP) on the physicochemical and structural properties of heat-induced whey protein isolate (WPI) gels, and explored the potential mechanism. The results indicated that STP promoted the unfolding and cross-linking of WPI to form a stable three-dimensional network structure, and significantly improved the strength, water-holding capacity and viscoelasticity of WPI gels. However, the addition of STP was limited to 2 %, too much STP would loosen the gel network and affect the gel properties. The results of FTIR and fluorescence spectroscopy suggested that STP affected the secondary and tertiary structures of WPI, promoted the movement of aromatic amino acids to the protein surface and the conversion of α-helix to β-sheet. In addition, STP reduced the surface hydrophobicity of the gel, increased the free sulfhydryl content, and enhanced the hydrogen bonding, disulfide bonding, and hydrophobic interactions between protein molecules. These findings can provide a reference for the application of STP as a gel modifier in the food industry.
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Molecular interactions including hydrophobic interaction, hydrogen bond, electrostatic interaction and disulfide bond, and secondary structures including α-helix, β-sheet, β-turn, and random coil, play a vital role in the maintenance of gel network.
“Molecular interactions including hydrophobic interaction, hydrogen bond, electrostatic interaction and disulfide bond, and secondary structures including α‐helix, β‐sheet, β‐turn, and random coil, play a vital role in the maintenance of gel network (M. Liu, Shan, et al. 2023).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
Excessive gelation agents or over-processing can disrupt intermolecular interactions, leading to weakened gel matrix.
“However, excessive gelation agents or over‐processing can disrupt the intermolecular interactions, leading to weakened gel matrix.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
Along with growth of β-sheet or reduction of α-helix contents in protein gels upon addition of polysaccharides, mechanical properties, rheological properties, and WHC were increased.
“Along with the growth of β‐sheet or the reduction of α‐helix contents in protein gels upon the addition of polysaccharides, mechanical properties (e.g., gel strength), rheological properties, and WHC were increased.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
Increased disulfide bonds consistently correlate with higher gel strength, G′/G′′ and water holding capacity, whereas reduced disulfide bond formation typically results in a weaker gel matrix.
“The increased disulfide bonds consistently correlate with higher gel strength, G′/G″ and water holding capacity (WHC), whereas the reduced disulfide bond formation typically results to a weaker gel matrix (M. Liu, Shan, et al. 2023; Teng et al. 2024; Song et al. 2025).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
β-sheet has been consistently linked to stronger gel performance, whereas α-helix correlates with weaker gel properties.
“β‐sheet has been consistently linked to stronger gel performance, whereas α‐helix correlates with weaker gel properties.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
Main secondary structure has been identified as either β-sheet or β-turn in heat-induced whey protein hydrogels.
“For example, the main secondary structure has been identified as either β‐sheet (H. Liu, Yang, et al. 2025) or β‐turn (M. Liu, Shan, et al. 2023) in the heat‐induced whey protein hydrogels.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
Disulfide bonds exhibit a strong positive association with gel mechanical properties.
“Notably, disulfide bonds exhibit a strong positive association with gel mechanical properties.”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Liu, Shan, et al. 2023
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“Aromatic amino acids in hydrophobic environments exhibited higher quantum yields, and the fluorescence intensity was significantly reduced when they moved from the core of the protein to a polar environment (Liu, Shan, et al., 2023).”
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- Authors
- Liu, M., Shan, S., Gao, X., Shi, Y., & Lu, W.
- Affiliations
- Harbin Institute of Technology (CN)
- Corresponding author
- Lu, Weihong
- Venue
- International Journal of Biological Macromolecules
- Publisher
- Elsevier BV
- Published
- 2023-06
- Volume
- 240
- Pages
- 124344
- ISSN
- 0141-8130 (ISSN-L)
- OpenAlex
- W4362635857
- Cited by
- 115
- References
- 0
- Citations by year
- 2026: 37 · 2025: 46 · 2024: 24 · 2023: 8
- FWCI
- 16.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- International Journal of Biological Macromolecules (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Heilongjiang Provincial Finance Department (HITTY-20190034)
- Ministry of Science and Technology of the People's Republic of China
- National Key Research and Development Program of China (2017YFC1601900)
- 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
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Keywords
- whey protein isolate, heat-induced gelation, gel structure, protein unfolding, protein cross-linking, water holding capacity, viscoelasticity, protein secondary structure, protein tertiary structure, surface hydrophobicity, disulfide bonds, hydrogen bonding
- MeSH terms
- Whey Proteins, Gels, Polysaccharides, Tea, Food Industry
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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