Peptides bitterness

If the Q-values lie between 13OO and 1400 no prediction can be made of the peptides bitterness. 

Bitterness occurs as a defect in dairy products as a result of casein proteolysis by enzymes that produce bitter peptides. Bitter peptides are produced in cheese because of an undesirable pattern of hydrolysis of milk casein (Habibi-Najafi and Lee 1996). According to Ney (1979), bitterness in amino acids and peptides is related to hydrophobic-ity. Each amino acid has a hydrophobicity value (Af), which is defined as the free energy of transfer of the side chains and is based on solubility properties (Table 7-6). The average hydrophobicity of a peptide, Q, is obtained as the sum of the Af of component amino acids divided by the number of amino acid residues. Ney (1979) reported that bitterness is found only in peptides with molecular weights... 

The production of bitter flavours generally is attributed to the formation of bitter peptides. Bitter flavour results when the peptides are formed faster than they can be broken down by the proteases and peptidase of the starter cultures. 

The water soluble portion was dialyzed and then freeze dried to yield bitter peptides. Bitter peptides from com gluten and casein were prepared in a similar manner. 

The enzymatic hydrolysates of milk casein and soy protein sometimes have a strong bitter taste. The bitter taste is frequently developed by pepsin [9001 -75-6] chymotrypsin [9004-07-3] and some neutral proteases and accounted for by the existence of peptides that have a hydrophobic amino acid in the carboxyhc terminal (226). The relation between bitter taste and amino acid constitution has been discussed (227). 

As a result of the en2ymatic degradation of proteins, key indexes change, ie, protein solubiUty indexes (PSI), peptide chain length (PCL), and protein solubihty in 0.8 Af TCA (TCA-index) (Fig. 14). Unpleasant bitterness was once a problem for some protein hydroly2ates. This problem can now be overcome by proper selection of the reaction parameters and the en2ymes used. 

The importance of lipophilicity to bitterness has been well established, both directly and indirectly. The importance of partitioning effects in bitterness perception has been stressed by Rubin and coworkers, and Gardner demonstrated that the threshold concentration of bitter amino acids and peptides correlates very well with molecular connectivity (which is generally regarded as a steric parameter, but is correlated with the octanol-water partition coefficient ). Studies on the surface pressure in monolayers of lipids from bovine, circumvallate papillae also indicated that there is a very good correlation between the concentration of a bitter compound that is necessary in order to give an increase in the surface pressure with the taste threshold in humans. These results and the observations of others suggested that the ability of bitter compounds to penetrate cell membranes is an important factor in bitterness perception. 

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). 

BTR) and "sour" (SOU), increase. Most "bitter" and "sour" flavors are thought to originate from the degradation/decomposition of proteins to bitter and sour flavored peptides and amino acids. 

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). 

Some attempts to reduce sodium chloride intake have been carried out. The first is to use some socUum chloride substitutes. Pottasium chloride is widely used for this purpose. However, pottasium chloride is not thought as perfect sodium chloride substitute because it contains bitter taste. Okai and his associates have synthesized several salty peptides (5). These peptides are expected to be good for hypertension, gestosis, diabetes mellitus and other deseases because they contain no sodium ions. These peptides, however, are not expected to be used as sodium chloride substitutes immediately because of the difficulty of in their synthesis and their cost. Although they are struggling to establish a new synthetic method of peptides in a mass production system with reasonable costs and to improve the salty potency of peptides, they have not dissolved this problem. Since the threshold value of ionic taste is around 1 mM regardless their kinds, it seems to be very difficult to prepare an artificial sodium... 

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. 

Bitterness of 0-Aminoacyl Sugars Containing Peptides Composed of Valine or Phenylalanine. Since hydrophobicity of the amino acid moiety seemed to be an important key for bitterness of 0-aminoacyl sugars, we then prepared O-... 

Stevenson et al. [62] studied the oligomerization of hydrophobic peptides such as Val-Leu, which are characterized by bitterness, with the aim of modifying peptide flavor. They found precipitation of oligomers in water/ethanol mixtures. By variation of the hydrophobicity of the model peptides, no significant product precipitation was observed in Gly-Gly, Ala-Gly, and Val-Gly. Product precipitation was observed for the more hydrophobic oligomers of Leu-Gly and Val-Leu. 

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