Interaction of synthetic proanthocyanidin dimer and trimer with bovine serum albumin and purified bean globulin fraction G-1

Abstract

To evaluate the type of binding involved, thermodynamic analysis of the temperature dependence of proanthocyanidin binding to bovine serum albumin (BSA) and bean glycoprotein G-l (G-l) was investigated. Binding was analyzed with tritiated proanthocyanidin by ultrafiltration to separate free ligand and protein-bound ligand. Binding constants were determined from Scatchard plots. Van't Hoff plots indicated proanthocyanidin binding to BSA was spontaneous and entropy driven. Analysis with cis-parinaric acid supported the conclusion drawn from the thermodynamic analysis that the binding of proanthocyanidin to BSA was a hydrophobic interaction. Van't Hoff plots indicated proanthocyanidin binding to native G-l protein was also spontaneous but, in contrast to BSA, enthalpy driven. Analysis with cis-parinaric acid confirmed the hydrophilic character of proanthocyanidin binding to native G-l. Evaluation of proanthocyanidin binding to heat-denatured G-l with cis-parinaric acid indicated hydrophobic interactions.

Factors affecting the nutritional value of pea (<i>Pisum sativum</i>) for broilers

“…These results are similar to those obtained by Smulikowska et al (2001) on birds and rats. According to Artz et al (1987), a high tannin content in peas may depress AA digestibility. The phenolic groups of tannins bind to enzymes and other proteins and form insoluble tannin-protein complexes resistant to the digestive enzymes of gastric animals; hydrogen bonds and hydrophobic interactions appear to be the principal linkages involved.…”

Tannin content affects negatively nutritive value of pea for monogastrics

“…It agrees well with reports of other authors (Lindgren, 1975;Gdala et al, 1992;Grosjean, 1999), who found significant differences in digestibility of protein between white-and coloured-flowered cultivars. The phenolic groups of tannins bind to enzymes and other proteins and form insoluble tanninprotein complexes resistant to digestive enzymes of monogastric animals, hydrogen bonds and hydrophobic interactions appear to be the principal linkages involved (Artz et al, 1987).…”

Binding of proanthocyanidins to soybean (Glycine max) seed ferritin inhibiting protein degradation by protease in vitro

“…Additionally, it was also reported that the interaction of salivary proteins and PAs (De Freitas and Mateus 2001) resulted in insoluble aggregates by hydrogen bonding and hydrophobic interactions between the two species (Artz, Bishop, Keith Dunker, Schanus, and Swanson 1987). Similarly, SSF is also rich in proline residues, and belonging to globular protein family, what will take place when meeting PAs?…”

“…Previous studies showed that the binding of PAs to a number of proteins such as salivary proteins (De Freitas and Mateus 2001) and BSA (Artz, Bishop, Keith Dunker, Schanus, and Swanson 1987) inhibited their degradation by proteases. This raises a question as to whether the binding of PAs to ferritin presented in this work likewise prevents ferritin from degradation by proteases in vitro.…”