Contribution of peptides and amino acids to the taste of foods

Abstract

The tastes of individual amino acids were characterized as being sweet, salty, sour, bitter, or MSG-like. The contribution of amino acids to the taste of various foodstuffs is discussed. The tastes of various peptides were characterized as being sour, bitter, or practically tasteless. Peptides from sake, soy sauce, and partial hydrolyzates of soybean protein were isolated and their tastes, as well as other properties, described.The importance of amino acids in contributing to the taste of foodstuffs was first recognized by Ikeda at Tokyo University in 1908 (Ikeda, 1908). He discovered that monosodium L-glutamate (MSG) was the essential component of the taste-imparting ingredients of traditional Japanese food seasoners, such as sea tangle (a type of seaweed). At that time the taste of traditional Japanese foods such as sake, miso, and soy sauce were presumed to be due to the amino acids which were released from the natural proteins during the course of fermentation. In addition, the taste of cheese had been known, in Europe and the United States, to be characterized by amino acids formed during the ripening process.

Caractérisation de l'emmental français "grand-cru". II. Analyses sensorielles

“…Preuve en est le cas de la forte corrélation (r = 0,593) entre la teneur en phénylalanine de la pâte et le caractère piquant des fro-treprise) a masqué l'effet de la teneur en sel sur le goût salé. Pour expliquer le lien assez étroit entre la saveur salée et les descripteurs de la protéolyse, il est possible de supposer que certaines fractions azotées ont un goût salé, ou bien que les peptides et les acides aminés (acides glutamique et aspartique, par exemple) qui agissent comme exhausteurs de goût pour cette saveur dans la plupart des aliments (Kirimura et al, 1969), ont aussi ce rôle dans les fromages.…”

Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition

“…7) Apart from steric factors, the si de chain hydrophobicity and hence the total amino acid hydrophobicity plays the most significant role in creating a perception of bitter taste (Ishibashi et al, 1988a). Threshold values of bitter amino acids leucine, tryptophan, phenylalanine, isoleucine, arginine, valine, methionine and histidine are listed in table VIII (Kirimura et al, 1969;Fujimaki et al, 1970a;Matoba et al, 1970). …”

“…lt has been observed that dipeptides containing neutral amino acids with either large alkyl groups (~C 3 ) or a combination of large and small (:5 C 2 ) alkyl groups, neutral and aromatic amino acids, or neutral and basic ami no acids, are bitter (Kirimura et al, 1969). One cause of bitterness lies in peptides, containing a high proportion of hydrophobic side-chains (proline, leucine and valine), as weil as of glutamic acid, with a ratio of aliphatic to acidic amino acids of 0.…”

Astringency, a textural defect in dairy products

“…ln order to analyse the chemical composition of Swiss cheese and to relate it to its characteristic taste, Swiss cheese samples have been fractionated into oil-soluble, water-soluble-volatile and water-solublenon-volatile components. This last fraction was found to contain astringent components which were further separated according to a modification of the procedure of Kirimura et al (1969). This process consisted of passing the water-soluble-non-volatile fraction through 5 successive Oowex 50 columns (20 x 200 mm) with decreasing degree of cross-linkage (x16, x12, x8, x4 and x2, respectively) to allow the separation of amino acids and peptides of different sizes.…”

“…According to L6pez-Fandiiio et al (1993), this RP-HPLC method could help to predict the risk of deterioration on storage of freshly prepared milks and would throw out a hint that the origin of astringency in UHT milk might not be due to whey proteins. Kirimura et al (1969), in their study on the contribution of peptides and amino acids to the taste of foodstuffs, found that dipeptides involving the y-COOH group of glutamic acid (Glu) in the peptide linkage are astringent. The assumption is supported by Nishimura and Kato (1988) who established that the peptides listed in table X are astringent.…”