Cited by 23Proteins in Food SystemsMicroencapsulation and Drying ProcessesFood composition and properties

Influence of rose anthocyanin extracts on physicochemical properties and in vitro digestibility of whey protein isolate sol/gel: Based on different pHs and protein concentrations

Wang, Yun, Yang, Cheng, Zhang, Jian, Zhang, Lianfu·2023·Food Chemistry

Abstract

Protein-polyphenol interactions can improve the physicochemical properties of proteins. The objective of this study was to investigate the influence of rose anthocyanin extracts (RAEs) on the physicochemical properties and digestibility of whey protein isolate (WPI) sol/gel at different pHs and protein concentrations. Hydrophobicity interaction and ionic bonding were the main forces for the formation of acidic WPI and WPI-RAEs sol/gel. When pH was higher than 2.4, sol/gel became unstable, which may be related to hydrophobicity, ζ-potential value, total sulfhydryl and free sulfhydryl content changes. In addition, RAEs had positive effects on the color and water distribution of all WPI sol/gel. Moreover, RAEs improved the viscoelasticity of WPI sol/gel with protein content ≥ 12 % (w/v) at pH 2.4. More importantly, the addition of RAEs could reduce the digestibility of WPI sol/gel. We hope our works can provide promising strategies for developing WPI-RAEs foods.

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Crossref · 10.1016/j.foodchem.2022.134937

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  • These structural changes limited the accessibility of digestive enzymes to target hydrolysis sites and inhibited enzyme diffusion within the gel matrix.

    “These structural changes limited the accessibility of digestive enzymes to target hydrolysis sites and inhibited enzyme diffusion within the gel matrix”

    From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Y. Wang, Yang, et al. 2023

  • The inhibitory effect of polyphenols on gel digestibility is primarily attributed to polyphenols-protein interactions (e.g., covalent grafting or non-covalent complexation), which promote formation of compact gel networks or insoluble polyphenol-protein aggregates.

    “This inhibitory effect is primarily attributed to polyphenols–protein interactions (e.g., covalent grafting or non‐covalent complexation), which promote the formation of compact gel networks or insoluble polyphenol–protein aggregates.”

    From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as Y. Wang, Yang, et al. 2023

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Authors
Wang, Y., Yang, C., Zhang, J., & Zhang, L.
Affiliations
  • Jiangnan University (CN)
  • Shihezi University (CN)
Corresponding author
Zhang, Lianfu
Venue
Food Chemistry
Publisher
Elsevier BV
Published
2023-03
Volume
405
Issue
Pt B
Pages
134937
ISSN
0308-8146 (ISSN-L)
OpenAlex
W4308808595
Cited by
22
References
40
Citations by year
2026: 4 · 2025: 5 · 2024: 6 · 2023: 7
FWCI
2.40
Type
journal article
Language
en
Open access
closed
Locations
  • Food Chemistry (publishedVersion)
  • PubMed (publishedVersion)
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
  • Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
Keywords
whey protein isolate, protein-polyphenol interactions, in vitro digestibility, pH effect, protein concentration, hydrophobic interactions, ionic bonding, zeta potential, sulfhydryl groups, viscoelasticity, water distribution, color, functional food development
MeSH terms
Whey Proteins, Anthocyanins, Food, Polyphenols

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