Sweet peptide

Some peptides have special tastes. L-Aspartyl phenylalanine methyl ester is very sweet and is used as an artificial sweetener (see Sweeteners). In contrast, some oligopeptides (such as L-ornithinyltaurine HQ. and L-oriuthinyl-jB-alariine HQ), and glycine methyl or ethyl ester HQ have been found to have a very salty taste (27). 

Sweetness is a quality that defies definition, but whose complexity can be appreciated merely by examining the molecular structures of those compounds that elicit the sensation. They come in all molecular shapes and sizes, and they belong to such seemingly unrelated classes of compounds as aliphatic and aromatic organic compounds, amino acids, peptides and proteins, carbohydrates, complex glycosides, and even certain inorganic salts. 

Gum acacia is a unique polysaccharide, with some peptides as part of the structure and has a range of different uses. It was originally the gum in gum sweets although some gum sweets do contain modified starch as a substitute. The replacement of gum is not because the substitute performs better but because there have been supply problems with gum acacia. Gum acacia is likely to be encountered in bakeries in small quantities when it has been used to make emulsions of citrus oils as a bakery flavour. It is possible to use gum acacia in making dry flavours from oils such as citrus by making an emulsion and then spray drying it. 

Sweetness Production by the Combination of Bitter and Sweet Tastes. Sensory tests using typically bitter compounds such as brucine, strychnine, phenylfiiiourea, caffeine and bitter peptides were performed. Sensory tests using typically bitter compounds such as brucine, strychnine, phenylthiourea, caffeine and bitter peptides were performed. Sensory taste impression were also measured for combinations of acetic acid (sour) and typical bitter compounds (5). The data from these studies indicated that the tastes of ese bitter/sour mixtures changed to a sweet taste regardless of their chemical structure of the bitter component (Table II). 

MW peptide fractions (7). Both the "fresh-cooked" and "cooked- -stored" samples resolve into separate regions, i.e., a hydrophilic region and a hydrophobic region. Hydrophilic peptides are commonly associated with flavors such as "sweet" and possibly, "meaty" and "cooked beef/brothy", whereas the hydrophobic peptides are usually associated with the more undesirable flavors like bitter" and "sour". 

Expansion or enhancement of the proposed mechanism of Nakamura and Okai is shown in Figure 12. Their model is based on the demonstration that several synthetically prepared di- and tri- peptide fragments composed of basic or acidic amino acids, produced individual tastes such as salty (lys-gfy sweet (lys-gfy-asp), sour (asp-glu-glu) and bitter (ser-leu-ala 31). Tlie expanded mechanism we propose is shown in Figure 12 and is based on the data tabulated in Table 1 (31, 38). 

Taste of Dipeptides Containing Lys and/or Gly. Since Lys-Gly HCl produces the saltiness, we prepared some dipeptides composed of Lys and/or Gly. The results are listed in Table XI. Gly-Lys, of which the amino acid sequence is opposite to the salty peptide Lys-Gly-HCl, produced a weakly sweet taste instead of the salty taste. Dipeptide composed of only Lys or Gly did not any taste. 

Today, it is well-known that peptides or proteins exhibit various kinds of taste. Our group has been researching on the relationship between taste and structure of peptides, BPIa (Bitter peptide la, Arg-Gly-Pro-Pro-Phe-Ile-Val) (7 as a bitter peptide, Om-p-Ala-HCl (OBA), Om-Tau-HCl as salty peptides(2j, and "Inverted-Aspartame-Type Sweetener" (Ac-Phe-Lys-OH) as a sweet peptide(5). The relationship between taste and chemical structure was partly made clear. Since commercial demand for these flavor peptides is increasing, we need to develop new synthetic methods which can prepare these peptides in large scale. We developed the following two methods (1) protein recombination method as a chemical method, (2) enzymatic synthesis using chemically modified enzyme as a biochemical method. 

The analysis, in composite over the four classes of L-aspartyl dipeptides suggests that the electron-withdrawing effect of substituents directed to the peptide bond, and the steric dimensions of the molecules, are important in eliciting the sweet taste. The values of the regression coefficients of the a term in the QSAR equations for L-aspartic acid amides, L-aspartylaminoethylesters, and L-aspartylaminopropionates all... 

Aspartame. Aspartame [22839-47-0] [53906-69-1] (APM, L-aspartyl-L-phenylalanine methyl ester) (1), also known under the trade names of NutraSweet and EQUAL, is the most widely used nonnutritive sweetener worldwide. This dipeptide ester was synthesized as an intermediate for an antiulcer peptide at G. D. Searle in 1965. Although this compound was known in the literature, its sweet taste was serendipitously discovered when a chemist licked his finger which was contaminated with it. Many analogues, especially the more stable esters, were made (6) and their taste qualities and potencies determined. It was the first compound to be chosen for commercial development. Following the purchase of G. D. Searle by Monsanto, the aspartame business was split off to become a separate Monsanto subsidiary called the NutraSweet Company. 

The multiple functions of peptides in foods (antioxidants, antimicrobial agents, surfactants) and their role in the development of characteristic flavors (sweetness, bitterness), as well as the information they can provide about the genuineness of foods, make peptide analysis a necessity. Producers as well as government laboratories have considerable interest in the study of peptides, both for research purposes and for the control of raw materials and manufactured foods. For this reason, substantial attention is now being focused on the development of analytical techniques designed to separate, characterize, and quantify peptides. 

Other peptides, such as L-aspartyl-L-phenylalanine methyl ester (aspartame), have a sweet taste. Several studies have been carried out to relate the structure and taste of analogs of this dipeptide (25). Tsang et al. (26) reported that the analogs at the lower end of the L-aspartyl-a-aminocycloalkanecarboxylic acid methyl ester series were sweet, the dipeptides containing a-... 

Aspartame. Aspartame is a widely used intense sweetener that has excellent taste characteristics, ft is a peptide made from two amino acids, phenylalanine and aspartic acid, but will in an acidic beverage medium slowly hydrolyse to its components. The fact that aspartame is a source of phenylalanine is of concern to consumers with certain complaints, and suitable label declarations are now required by law. Technically, this slow hydrolysis brings about loss of sweetness. 

Wine is one of the most complex and interesting matrices for a number of reasons. It is composed of volatile compounds, some of them responsible for the odor, and nonvolatile compounds which cause taste sensations, such as sweetness (sugars), sourness (organic acids), bitterness (polyphenols), and saltiness (mineral substances Rapp and Mandary, 1986). With a few exceptions, those compounds need to be present in levels of 1%, or even more, to influence taste. Generally, the volatile components can be perceived in much lower concentrations, since our organs are extremely sensitive to certain aroma substances (Rapp et ah, 1986). Carbohydrates (monosaccharides, disaccharides, and polysaccharides), peptides, proteins, vitamins, and mineral substances are among the other wine constituents. 

The sweet dipeptide esters of the L-aspartic acid and the L-amino malonic acid (15-21) are interesting exceptions to the bitter taste shared by all other members of the peptide series. Fig. 

After the finding of a sweet taste in L-Asp-L-Phe-OMe (aspartame) by Mazur et at. (6), a number of aspartyl dipeptide esters were synthesized by several groups in order to deduce structure-taste relationships, and to obtain potent sweet peptides. In the case of the peptides, the configuration and the conformation of the molecule are important in connection with the space-filling properties. The preferred conformations of amino acids can be shown by application of the extended Hiickel theory calculation. However, projection of reasonable conformations for di- and tripeptide molecules is not easily accomplished. 

In the course of investigations of aspartyl dipeptide esters, we had to draw their chemical structures in a unified formula. In an attempt to find a convenient method for predicting the sweettasting property of new peptides and, in particular, to elucidate more definite structure-taste relationships for aspartyl dipeptide esters, we previously applied the Fischer projection technique in drawing sweet molecules in a unified formula 04). 

The sweet-tasting property of aspartyl dipeptide esters has been successfully explained on the basis of the general structures shown in Figure 1 (4). A peptide will taste sweet when it takes... 

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