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Mechanisms of Protein Precipitation for Two Tannins, Pentagalloyl Glucose and Epicatechin16 (4→8) Catechin (Procyanidin)
Abstract
The precipitates that form when purified pentagalloylglucose or a purified procyanidin [epicatechin 16 (4→8) catechin; EC 16 -C] are mixed with bovine serum albumin were quantitatively analyzed. EC 16 -C is a more efficient protein precipitating agent than pentagalloylglucose on a molar or a mass basis. EC 16 -C precipitates protein independently of temperature and presence of organic solvent. Precipitation by pentagalloylglucose increases as temperature is increased and decreases when alcohols are present. When tannin is in excess, up to 40 mol of pentagalloylglucose is bound per mole of protein precipitated, but only 20 mol of EC 16 -C is bound per mole of protein precipitated. The data support different models of precipitation for the two types of tannin: pentagalloylglucose, which is very nonpolar, precipitates by forming a hydrophobic coat around the protein, whereas the much more polar EC 16 -C forms hydrogen-bonded cross-links between protein molecules. Keywords: Polyphenol−protein interaction; tannin; pentagalloylglucose; procyanidin; condensed tannin; bovine serum albumin
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Cited by
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Mueller‐Harvey, I. (2006) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.2577 · Cited by 965
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Zhang, J., Li, L., Kim, S.-H., Hagerman, A. E., & Lü, J. (2009) · Pharmaceutical Research · doi:10.1007/s11095-009-9932-0 · Cited by 294
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Roopchand, D. E., Krueger, C. G., Moskal, K., Fridlender, B., Lila, M. A., & Raskin, I. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.06.050 · Cited by 73
Metadata
- Authors
- Hagerman, A. E., Rice, M. E., & Ritchard, N. T.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1998-05-20
- Volume
- 46
- Issue
- 7
- Pages
- 2590-2595
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W1975109027
- Cited by
- 361
- References
- 0
- FWCI
- 1.01
- Type
- journal article
- Language
- en
- Open access
- closed
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