Interaction of (+)-catechin, (?)-epicatechin, procyanidin B2 and procyanidin C1 with pooled human salivain vitro

Καλλιθράκα, Σταματίνα; Clifford, Michael N.

doi:10.1002/1097-0010(20010115)81:2<261::aid-jsfa804>3.0.co;2-t

Cited by 33 publications

(7 citation statements)

References 28 publications

(42 reference statements)

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“…Even well-trained panelists might confuse bitterness and astringency or have difficulties distinguishing between them. 14 Therefore, an objective analytical tool to measure the quality of astringency is of greatest importance not only to assess the quality of foodstuffs but also to elucidate the nature and binding of astringent substances. Different approaches to assess astringency have been published during the past years.…”

Section: Introductionmentioning

confidence: 99%

“…21 In a recent study, it could be shown that the amount of precipitates could not be compared with the relative astringency reported from the taste panelists. 14 Therefore, a method, which does not only rely on precipitation of the protein, may be of great interest to elucidate the problem of astringency. Immobilization of the protein on a solid inert matrix is definitely an interesting approach, because soluble complexes can also be evaluated.…”

Section: Introductionmentioning

confidence: 99%

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Toward the Optical Tongue: Flow-Through Sensing of Tannin−Protein Interactions Based on FTIR Spectroscopy

2002

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The interaction of polyphenols (tannins) with proline-rich proteins (gelatin) has been studied using an automated flow injection system with Fourier transform infrared spectroscopic detection to gain insight into chemical aspects related to astringency. In the perception of astringency, a major taste property in red wines and other beverages such as beer, tea, or fruit juices, an interaction between proline-rich salivary proteins and tannins present in the sample takes place. To study this interaction, agarose beads carrying gelatin (a proline-rich protein) were placed in the IR flow cell in such a way that the beads were probed by the IR beam. Using an automated flow system, we injected samples in a carrier stream and flushed over the proteins in a highly reproducible manner. Simultaneously, any retardation due to tannin-protein interactions taking place inside the flow cell was monitored by infrared spectroscopy. Tannins of different sources (grapes, wooden barrels, formulations used in wine making) were investigated, and their flow-through behavior was characterized. Significant differences in their affinity toward gelatin could be observed. Furthermore, because of small but characteristic differences in the IR spectrum, it is possible to distinguish condensed from hydrolyzable tannins. Nonastringent substances such as alcohols, sugars, and acids did not show retention on gelatin. The selectivity of the flow-through sensor was also demonstrated on the example of red and white wine. In contrast to white wine, where no interaction could be observed, in red wine a major interaction of the red wine tannins was found.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Toward the Optical Tongue: Flow-Through Sensing of Tannin−Protein Interactions Based on FTIR Spectroscopy

2002

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“…It is important to note that PRPs bind specifically to tannins [43, 47–52] (Table 1), and with an increased affinity compared to digestive enzymes and proteins [4, 53], which supports the role of PRPs serving as biological protectors against tannins. Selectivity is regulated by both tannin and PRP properties enhancing binding affinity; high-affinity tannin molecules are bound first, then lower affinity molecules are bound at higher concentrations [54]. Enzyme activity inhibited by tannins is enhanced in the presence of PRPs, pointing to tannin-PRP preferential binding [52], and similarly structured compounds to PRPs have not been found to bind to tannins with the robust affinity found in tannin-PRP binding [50].…”

Section: Resultsmentioning

confidence: 99%

Salivary proline-rich protein may reduce tannin-iron chelation: a systematic narrative review

et al. 2017

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BackgroundTannins are often cited for antinutritional effects, including chelation of non-heme iron. Despite this, studies exploring non-heme iron bioavailability inhibition with long-term consumption have reported mixed results. Salivary proline-rich proteins (PRPs) may mediate tannin-antinutritional effects on non-heme iron bioavailability.AimTo review evidence regarding biochemical binding mechanisms and affinity states between PRPs and tannins, as well as effects of PRPs on non-heme iron bioavailability with tannin consumption in vivo.MethodsNarrative systematic review and meta-analysis. Common themes in biochemical modeling and affinity studies were collated for summary and synthesis; data were extracted from in vivo experiments for meta-analysis.ResultsThirty-two studies were included in analysis. Common themes that positively influenced tannin-PRP binding included specificity of tannin-PRP binding, PRP and tannin stereochemistry. Hydrolyzable tannins have different affinities than condensed tannins when binding to PRPs. In vivo, hepatic iron stores and non-heme iron absorption are not significantly affected by tannin consumption (d = −0.64-1.84; −2.7-0.13 respectively), and PRP expression may increase non-heme iron bioavailability with tannin consumption.ConclusionsIn vitro modeling suggests that tannins favor PRP binding over iron chelation throughout digestion. Hydrolyzable tannins are not representative of tannin impact on non-heme iron bioavailability in food tannins because of their unique structural properties and PRP affinities. With tannin consumption, PRP production is increased, and may be an initial line of defense against tannin-non-heme iron chelation in vivo. More research is needed to compare competitive binding of tannin-PRP to tannin-non-heme iron complexes, and elucidate PRPs’ role in adaption to non-heme iron bioavailability in vivo.Electronic supplementary materialThe online version of this article (doi:10.1186/s12986-017-0197-z) contains supplementary material, which is available to authorized users.

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“…For example, the precipitation of catechin and epicatechin at different flavanol concentrations and at different flavanol solution/saliva ratios was shown. 43 Concerning hydroxycinnamic acids, precipitation of CQA oxidation products in the presence of salivary proteins (particularly cystatins and P−B peptide) was demonstrated. 45 Here, the pH conditions (5.4) and the limited time of contact between saliva and the polyphenol extract (10 min incubation +10 min centrifugation) cannot be considered as highly favorable to oxidation.…”

Section: ■ Discussionmentioning

confidence: 99%

Interactions between Salivary Proteins and Apple Polyphenols and the Fate of Complexes during Gastric Digestion

Berkel Kasikci,

Guilois-Dubois,

Billet

et al. 2024

J. Agric. Food Chem.

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Beneficial polyphenols in apples can reach the stomach as complexes formed with salivary proteins. The present study aimed at documenting the interactions between salivary proteins and cider apple polyphenols and the fate of complexes during gastric digestion. A polyphenolic extract was mixed with human saliva, and interactions were characterized by analyzing proteins and polyphenols in the insoluble and soluble fractions of the mixtures, before and after in vitro gastric digestion. Results confirmed that proline-rich proteins can efficiently precipitate polyphenols and suggested that two zinc-binding proteins can also form insoluble complexes with polyphenols. The classes of polyphenols involved in such complexes depended on the polyphenol-to-protein ratio. In vitro gastric digestion led to extensive proteolysis of salivary proteins, and we formulate the hypothesis that the resulting peptides can interact with and precipitate some procyanidins. Saliva may therefore partly modulate the bioaccessibility of at least procyanidins in the gastric compartment.

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Interaction of (+)-catechin, (?)-epicatechin, procyanidin B2 and procyanidin C1 with pooled human salivain vitro

Cited by 33 publications

References 28 publications

Toward the Optical Tongue: Flow-Through Sensing of Tannin−Protein Interactions Based on FTIR Spectroscopy

Toward the Optical Tongue: Flow-Through Sensing of Tannin−Protein Interactions Based on FTIR Spectroscopy

Salivary proline-rich protein may reduce tannin-iron chelation: a systematic narrative review

Interactions between Salivary Proteins and Apple Polyphenols and the Fate of Complexes during Gastric Digestion

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