Effects of galloyl group on the astringency perception of epigallocatechin gallate and epigallocatechin.

Zhenyu Zhou, Qian Huang, Wangyang Shen, Weiping Jin, Guoyan Yang, Wenjing Huang, Cheng Guo

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Article in Current research in food science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Elucidating the astringency perception mechanism of protocatechuic acid, a key astringent component in black rice, based on polyphenol-salivary protein interaction.Current research in food science · 2026
Article

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5 · Who and what money

Authors and funding

7 authors.

Zhenyu ZhouCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Qian HuangCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Wangyang ShenCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Weiping JinCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Guoyan YangCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Wenjing HuangCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Cheng GuoCollege of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The astringency in green tea primarily originates from gallate-type and non-gallate-type catechins. Epigallocatechin gallate (EGCG) is a gallate-type catechin, which has a strong astringency and is the most abundant catechin in tea. Unlike EGCG, epigallocatechin (EGC) has one fewer galloyl group on the C3 oxygen atom and exhibits a weaker astringency. Taking EGCG and EGC as representative catechins, this study investigated the effects of the galloyl group on their astringency. The interactions of EGCG and EGC with salivary proteins were qualitatively and quantitatively analyzed using fluorescence spectroscopy, isothermal titration calorimetry, and molecular docking. The surface roughness and viscoelasticity of the salivary film were then studied to relate the molecular interactions and perceived astringency. Additionally, the bindings of EGCG and EGC to astringency receptor proteins were also simulated. The results revealed that the galloyl group enabled the EGCG-promoted aggregation of salivary proteins, resulting in a stronger astringency through both tactile and gustatory pathways. In contrast, EGC exhibited a weaker astringency only through the gustatory pathway.

Indexed as

Astringency receptorEpigallocatechinEpigallocatechin gallateMolecular interactionSalivary filmSalivary protein

Identifiers

PMID40612443

DOI10.1016/j.crfs.2025.101120

PMCPMC12226114

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.