The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Nature of Polyphenol−Protein Interactions
Abstract
Proteins and polyphenols were combined in model systems, and the resulting hazes were measured by light scattering. The amount of haze formed depends both on the concentrations of protein and polyphenol and on their ratio. A conceptual model in which a protein molecule has a fixed number of polyphenol binding sites explains the observed behavior and has implications for turbidimetric methods for estimating haze-active protein and haze-active polyphenol in beverages. The ranking of haze-forming activity of the test polypeptides was different with tannic acid than with catechin; this indicates differences in binding site availability, bridging ability, or specificity for the two polyphenols. More haze was observed when model systems were heated, suggesting that polyphenol binding sites are exposed when protein hydrogen bonds are broken. Freshly formed haze dissolved when dimethylformamide or dioxane was added; this may be useful for recovering compounds from isolated hazes for analysis. Keywords: Haze-active protein; haze-active polyphenol; beverages; model systems; gelatin; tannic acid
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Cites
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Formation of complexes between protein and tannic acid
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The Chemical Nature and Precursors of Clarified Apple Juice Sediment
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New hydrophobic lipid interactions in tea cream
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Photoactivatable time-temperature indicators for low-temperature applications
Bhattacharjee, H. R. (1988) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00081a029 · Cited by 8
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Polyphenol‐Containing Nanoparticles: Synthesis, Properties, and Therapeutic Delivery
Guo, Y., Sun, Q., Wu, F., Dai, Y., & Chen, X. (2021) · Advanced Materials · doi:10.1002/adma.202007356 · Cited by 650
A single dose of tea with or without milk increases plasma antioxidant activity in humans
Leenen, R., Roodenburg, A., Tijburg, L., & Wiseman, S. (2000) · European Journal of Clinical Nutrition · doi:10.1038/sj.ejcn.1600900 · Cited by 347
Pateiro, M., Barba, F. J., Domínguez, R., Sant'Ana, A. S., Mousavi Khaneghah, A., Gavahian, M., Gómez, B., & Lorenzo, J. M. (2018) · Food Research International · doi:10.1016/j.foodres.2018.07.014 · Cited by 328
Tannins in Food: Insights into the Molecular Perception of Astringency and Bitter Taste
Soares, S., Brandão, E., Guerreiro, C., Soares, S., Mateus, N., & de Freitas, V. (2020) · Molecules · doi:10.3390/molecules25112590 · Cited by 308
A review on astringency and bitterness perception of tannins in wine
Ma, W., Guo, A., Zhang, Y., Wang, H., Liu, Y., & Li, H. (2014) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2014.08.001 · Cited by 306
Xiao, J., & Kai, G. (2012) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2010.499017 · Cited by 256
Supramolecular design and applications of polyphenol-based architecture: A review
Liang, H., Zhou, B., Wu, D., Li, J., & Li, B. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.102019 · Cited by 98
Naknean, P. (2013) · Journal of Food Safety · doi:10.1111/jfs.12084 · Cited by 15
Metadata
- Authors
- Siebert, K. J., Troukhanova, N. V., & Lynn, P. Y.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1996-01-01
- Volume
- 44
- Issue
- 1
- Pages
- 80-85
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2085052208
- Cited by
- 677
- References
- 5
- FWCI
- 16.59
- Type
- journal article
- Language
- en
- Open access
- closed
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