Cited by 115Proteins in Food SystemsPolysaccharides Composition and ApplicationsFood composition and properties

The effect of sweet tea polysaccharide on the physicochemical and structural properties of whey protein isolate gels

Liu, Mengyao, Shan, Shan, Gao, Xin, Shi, Yudong, Lu, Weihong·2023·International Journal of Biological Macromolecules

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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Crossref · 10.1016/j.ijbiomac.2023.124344

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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

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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
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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