Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0235290 (bitter taste)
 1,408 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

For the identification of a peptidyl principle inducing sexual agglutination in the yeast, 2 supposed hexapeptides (1a, b) were synthesized by the conventional method. The 1a (H-Arg-Gly-Pro-Phe-Pro-Ile-OH) revealed complete identity with the natural peptide in TLC, MS and biological property on agglutination. The 1b showed the sexual agglutinability in the same degree as 1a, though distinct differences were observed in the chemical data. Both 1a and 1b had a strong bitter taste.
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PMID:Synthetic identification as a hexapeptide of alpha substance-IB inducing sexual agglutination in Saccharomyces cerevisiae. 33 Jan 97

About 80 peptides and their derivatives were tested for bitter taste. The taste thresholds are in the range of 70-80 muMol/ml (Gly-Val) to 0.01-0.02 muMol/ml (Bacitracin). They are dependent on nature and number of the side chains and on the hydrophobicity of the whole molecule. An estimation of the taste thresholds of all di-and tripeptides with known amino acid composition is possible on the basis of their hydrophobicity. As could be shown recently for bitter amino acids, a polar (electrophilic) and a hydrophobic group are essential requirements for bitter peptides also. This model corresponds to all sensory results, e.g. to the bitter taste of all hydrophobic peptides independent on their sequence and configuration and to the sweet taste of L-aspartyl dipeptide esters.
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PMID:[Relations between structure and bitter taste of amino acids and peptides. II. Peptides and their derivatives (author's transl)]. 97 40

Eight peptides with bitter taste were isolated from a hydrolyzate of the corn protein zein using several chromatographic procedures. The peptides have the following amino acid sequences and taste thresholds (muM/ml): Ala-Ile-Ala (50-100), Ala-Ala-Leu (50-100), Gly-Ala-Leu (50-100), Leu-Glu-Leu (2.5-3.5), Leu-Glu-Leu (8-12), Leu-Val-Leu (1.5-2.5), Leu-Pro-Phe-Asn-Gln-Leu (0.1-0.2), Leu-Pro-Phe-Ser-Gln-Leu (0.1-0.2). The threshold for bitter taste decreases with increasing number of hydrophobic side chains (greater than or equal to C3) in the peptide. It increases in the presence of hydrophilic side chains to their polarity.
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PMID:[Bitter peptides isolated from corn protein zein by hydrolysis with pepsin (author's transl)]. 122 27

The cell-associated peptidase profiles of 12 strains of Pseudomonas fluorescens (ATCC 948 and 11 related biotypes) were examined. Employing Analytab system API ZYM, a general, strong peptidase activity was detected using L-lysyl-, L-pyrrolidonyl-, L-arginyl-, L-alanyl-, and glycyl-glycyl-beta-naphthylamides as substrates. Conversely, L-tyrosyl-, L-phenylalanyl-, L-histidyl-, L-prolyl-, gamma-L-glutamyl-beta-naphthylamides substrates were hydrolyzed by only a few strains. The peptidases were active, therefore, on substrates responsible for the bitter taste in dairy products. Properties of hydrolytic systems showed no significant changes in the enzymatic profiles when cells were grown on different fermentation media. Enzyme activity was relatively stable during refrigerated (5 degrees C) and frozen (-18 degrees C) storage. The peptidases of P. fluorescens ATCC 948, considered as reference, and strain 22 were identified on Pro-beta-naphthylamides by Michaelis constant values of .528 and .394 mM, respectively, and by different optimal pH and temperature activity on Leu- and Pro-beta-naphthylamides. The peptidase activity on Gly-Phe-beta-naphthylamide in P. fluorescens 30 had optimal values at pH 7.50 and 45 degrees C. These results confirm the relations defined in the enzymatic identification phase and suggest the presence of any analogous peptidases in the biovars of P. fluorescens considered.
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PMID:Peptidase profiles of Pseudomonas fluorescens: identification and properties. 157 30

Activity-directed fractionation of heated carbohydrate/alanine solutions recently led to the discovery of (+)-(S)-1-(1-carboxyethyl)-5-hydroxy-2-(hydroxymethyl)pyridinium inner salt (1, alapyridaine), and it has been shown that this compound lowers the detection thresholds of sugars, glutamate, and NaCl solutions, whereas no influence on bitter perception was observed. As this class of Maillard-derived pyridinium betaines seemed to be promising targets for further research on their taste modulatory activity, the objective of the present investigation was to screen for bitter taste-suppressing target molecules in combinatorial libraries of pyridinium betaines prepared from 5-(hydroxymethyl)furan-2-aldehyde and amino acid mixtures by use of Maillard-type reaction chemistry instead of synthesizing and purifying each derivative individually. By application of hydrophilic interaction liquid chromatography in combination with the recently developed comparative taste dilution analysis, followed by structure determination, synthesis, and sensory studies, we have now succeeded in identifying 1-carboxymethyl-5-hydroxy-2-hydroxymethylpyridinium inner salt (2) as a potential bitter-suppressing candidate. While tasteless on its own, 2 was found to reduce the bitterness of various bitter tastants such as the amino acid L-phenylalanine, the peptide Gly-Leu, the alkaloid caffeine, and the bitter glycosides salicin and naringin.
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PMID:Application of hydrophilic interaction liquid chromatography/comparative taste dilution analysis for identification of a bitter inhibitor by a combinatorial approach based on Maillard reaction chemistry. 1627 18

Riboflavin-binding protein (RBP) from chicken egg, which was recently reported to be a selective sweet inhibitor for protein sweeteners, was also found to be a bitter inhibitor. RBP elicited broadly tuned inhibition of various bitter substances including quinine-HCl, naringin, theobromine, caffeine, glycyl-L-phenylalanine (Gly-Phe), and denatonium benzoate, whereas several other proteins, such as ovalbumin (OVA) and beta-lactoglobulin, were ineffective in reducing bitterness of these same compounds. Both the bitter tastes of quinine and caffeine were reduced following an oral prerinse with RBP. It was found that RBP binds to quinine but not to caffeine, theobromine, naringin, and Gly-Phe. However, the binding of RBP to quinine was probably not responsible for the bitter inhibition because OVA bound to quinine as well as RBP. Based on these results, it is suggested that the bitter inhibitory effect of RBP is the consequence of its ability to interact with taste receptors rather than because it interacts with the bitter tastants themselves. RBP may have practical uses in reducing bitterness of foods and pharmaceuticals. It may also prove a useful tool in studies of mechanisms of bitter taste.
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PMID:Riboflavin-binding protein is a novel bitter inhibitor. 1784 99

Fermented food contains numerous peptides derived from material proteins. Bitter peptides formed during the fermentation process are responsible for the bitter taste of fermented food. We investigated whether human bitter receptors (hTAS2Rs) recognize bitterness of peptides with a heterologous expression system. HEK293 cells expressing hTAS2R1, hTAS2R4, hTAS2R14, and hTAS2R16 responded to bitter casein digests. Among those cells, the hTAS2R1-expressing cell was most strongly activated by the synthesized bitter peptides Gly-Phe and Gly-Leu, and none of the cells was activated by the non-bitter dipeptide Gly-Gly. The results showed that these bitter peptides, as well as many other bitter compounds, activate hTAS2Rs, suggesting that humans utilize these hTAS2Rs to recognize and perceive the structure and bitterness of peptides.
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PMID:Bitter peptides activate hTAS2Rs, the human bitter receptors. 1803 73

Taste-taste interactions often showed in human psychophysical studies. Considering that each tastant in foodstuffs individually stimulates its responsible gustatory systems to elicit relevant taste modalities, taste-taste interaction should be performed in taste receptor cell-based assay. While umami substances have been proposed to suppress the bitterness of various chemicals in human sensory evaluation, the bitter-umami interaction has not been explored in bitter taste receptors, TAS2Rs. We investigated umami-bitter taste interactions by presenting umami peptides with bitter substance (salicin) on Ca(2+)-flux signaling assay using hTAS2R16-expressing cells. Five representative umami peptides (Glu-Asp, Glu-Glu, Glu-Ser, Asp-Glu-Ser, and Glu-Gly-Ser) derived from soybean markedly attenuated the salicin-induced intracellular calcium influx in a time-dependent manner, respectively, while Gly-Gly, a tasteless peptide did not. The efficacies of Glu-Glu suppressing salicin-induced activation of hTAS2R16 were higher than that of probenecid, a specific antagonist of hTAS2R16. According to Ca(2+)-flux signaling assay using the mixtures of salicin and umami peptides, all five umami peptides suppressed salicin-induced intracellular calcium influx in a noncompetitive manner. These results may provide evidence that umami peptides suppress bitter taste via bitter taste receptor(s). This is the first report which defines the interaction between bitter and umami taste in taste receptor level.
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PMID:Umami-bitter interactions: the suppression of bitterness by umami peptides via human bitter taste receptor. 2549 Mar 85