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Tannin—Protein Interactions

Hagerman, Ann E.·1992·ACS Symposium Series

Abstract

Over the last 20 years, information about the diverse compounds classified as "tannins" has rapidly accumulated. Structural studies have revealed that "tannins" belong to one of three groups of compounds: proanthocyanidins, gallotannins or ellagitannins. Each of the three types of tannin interacts strongly with protein, and a variety of approaches have been used to probe this characteristic reaction. The interaction is influenced by characteristics of the protein (including size, amino acid composition, pI, and extent of posttranslational modification), characteristics of the tannin (size, structure, heterogeneity of the preparation), and conditions of the reaction (pH, temperature, solvent composition, time). Under some conditions an insoluble complex is formed, but soluble complexes may also form. Both soluble and insoluble complexes are stabilized by reversible, noncovalent bonds between tannin and protein.

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Metadata

Authors
Hagerman, A. E.
Venue
ACS Symposium Series
Published
1992-10-01
Volume
213
Pages
236-247
ISSN
  • 0097-6156 (ISSN-L)
  • 1947-5918
OpenAlex
W123527290
Cited by
222
References
0
FWCI
2.82
Type
conference paper
Language
en
Open access
closed

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CoChat. (2026). Citation check: Tannin—Protein Interactions. https://app.cochat.ai/papers/10.1021/bk-1992-0506.ch019
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Hagerman, A. E. (1992). Tannin—Protein Interactions. ACS Symposium Series. https://doi.org/10.1021/bk-1992-0506.ch019

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