Sweetness Potency Research Articles

Structure-taste Relationship of Novel α-l-Aspartyl Dipeptide Sweetners

Abstract A sweetness potency was found in novel α-l-aspartyl dipeptide analogs which were quite stable on heating in an aqueous solution. The insertion of a methylene group into the peptide chain of α-l-aspartyl dipeptide esters mostly decreased the potency of the sweetness. However, the further exchange of the carbonyl and oxygen functions with each other on the ester group of a C-terminal β-alkyl-β-aminopropionic acid was found to increase the sweetness. Thus, N-(α-l-aspartyl)-O-pivaroyl-d-alaninol, N-(α-l-aspartyl)-O-cyclobutylcarbonyl-d-alaninol and N-(α-l-aspartyl)-O-cyclopropylcarbonyl-d-alaninol were all more than 200 times as sucrose.

Saccharin sodium as a potential sweetener for antidotal charcoal

This study explored if saccharin sodium, as a sweetener in activated charcoal formulations, would be sufficiently available to provide sweetness while not severely reducing charcoal's adsorption capacity. In vitro tests showed that charcoal takes up 40wt% of saccharin at a 1 g/liter concentration of saccharin in the residual fluid; 29.3wt% at 0.1 g/liter. A saccharin level of 0.1 g/g of charcoal in a carboxymethylcellulose formulation gave enough residual flavor to be appealing. Sodium salicylate, 1 g/liter and 10 g/liter, was used to test whether the 0.1 g/g level of saccharin would interfere with charcoal's ability to adsorb a typical drug. By use of colorimetric assay, it was shown that a 2 g charcoal per gram of salicylate (initial salicylate concentration of 1 g/liter), the extent of drug adsorption was reduced from 70% to 64%, at a 10 g/liter initial concentration, the reduction was 87% to 82%. Under the conditions tested, the antidotal mixture should be pleasantly sweet at a saccharin level of 1 g/10g charcoal, and little effect would be produced on the adsorption of sodium salicylate and other drugs that are well adsorbed by charcoal.

Structure-taste relationships of L-aspartyl-aminomalonic acid diesters.

L-Aspartyl-aminomalonic acid diesters are representatives of new group of sweet compounds. Chemical synthesis of the dipeptide esters was effected by coupling carbobenzoxy-β-benzylaspartic acid with an aminomalonic acid diester by the conventional activated ester method, followed by catalytic hydrogenation to remove the protecting groups. Among the 21 products, trans-2-methyl-cyclohexyl, methyl diester was over 5000 times sweeter than sucrose, 2, 6-dimethyl-cyclohexyl, methyldiester was about 5000 times sweeter and fenchyl, methyl diester was over 20000 times sweeter. These compounds appear to be the most potent sweeteners known of either natural or synthetic origin. On the basis of the potencies of the products, structure-taste relations in the C-terminal part of this molecule were discussed in detail.

The structure-taste relationships of aspartyl dipeptide esters.

The molecular features common to sweet-tasting dipeptide esters are described. The molecular features of sweet amino acids were represented by the Fischer projection formulas and sweet peptides were related to the sweet amino acids through the Fischer projection formulas of the peptides. It was concluded that a peptide is sweet when it takes the formula 5a, whereas when it takes the formula 5b it is not sweet. It was also concluded that a third binding site (R1 in 5a) besides the postulated AH–B system in a sweet molecule is necessary for an intense sweetness potency. The location of the site in the molecule relative to the AH–B system is important, as well as the shape and size of this site, because the third binding site is considered to participate in hydrophobic interaction with a similar binding site on the taste receptor. Increased sweetness is observed when these requirements are satisfied.

The Structure-Taste Relationships of the Dipeptide Esters Composed of l-Aspartic Acid and β-Hydroxy Amino Acids

Abstract In order to evaluate the contribution of a hydroxyl group to the degree of sweetness of aspartyl dipeptides, we have synthesized a number of α-l-aspartyl dipeptides, such as the esters of α-l-aspartyl-l-hydroxynorleucine (16 and 17), -O-acyl-l-serine (18–21), -d-serine (22–28), -d-threonine (30–36), and -d-allothreonine (37–43); their sweetness potencies were compared with those of the corresponding dipeptides without a hydroxyl group. It has been found that a hydroxyl group makes a major contribution to the sweetness of the α-l-aspartyl dipeptide esters. Trie introduction of a hydroxyl group into the l-l peptides gave compounds with reduced potency. However, no such regularity was observed in the l–d peptides; the esters of α-l-aspartyl-d-serine (22–28) and -d-threonine (30–36) were sweeter than the corresponding esters of α-l-aspartyl-d-alanine and -d-α-amino-n-butyric acid respectively, while the esters of α-l-aspartyl-d-allothreonine (37–43) were less sweet than the corresponding esters of α-l-aspartyl-d-α-amino-n-butyric acid. The enzymatic resolution of N-acetyl-erythro- and -threo-β-hydroxy-Dl-norleucine is also described.

Oxathiazinone Dioxides—A New Group of Sweetening Agents

Abstract1,2,3‐0xathiazin‐4(3H)‐one 2,2‐dioxides bearing lower alkyl substituents on C‐5 and C‐6 represent potential sweeteners. They are formed from chloro‐ or fluorosulfonyl isocyanate and acetylenes, ketones, β‐diketones, β‐oxo carboxylic esters, or benzyl vinyl ethers via N‐halosulfonyl β‐oxo carboxamides as common intermediates.