Umami Essay

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Sweetness. Lower molecular weight amino acids, except proline, are sweet irrespective of their configuration, and D-enantiomers of high molecular weight amino acids are generally sweet (Kemp & Birch, 1989). D-amino acids do not occur naturally but may be produced during food processing due to racemisation. There are currently no known natural peptides with a sweet taste (Weir, 1992). The synthetic peptide most recognised for its taste is L-aspartyl-L-phenylalanine methyl ester, i.e. aspartame, a low-caloric sweetener that is 180 times sweeter than sucrose. While several high molecular weight polypeptides are naturally sweet, their properties relate to the shape and electronic configuration of a large surface area rather than the peptide …show more content…

Umami may be defined as a pleasant savoury, meaty taste representative of the amino acid L-glutamate and 5’-ribonucleotides (Yamaguchi & Ninomiya, 2000). Free glutamate occurs naturally in a wide array of animal and plant foodstuffs such as meats, cheeses and vegetables, and is particularly abundant in Parmesan cheese and ripe tomatoes (Kurihara, 2009). Two key characteristics distinguish umami from other basic tastes: a taste-enhancing synergism between L-glutamate and 5’-ribonucleotides and a prolonged aftertaste (Ikeda, 1909). Lioe et al. (2006) reported that free glutamic acid and aspartic acid were the major contributors to the development of umami in soy sauce. However, while umami is known to enhance the palatability of foods by altering taste perceptions and provide roundedness to flavour (Beauchamp, 2009), data relating the effect of umami on the thresholds of other basic tastes are inconsistent. Mosel and Kantrowitz (1952) reported that MSG lowered the threshold values for sour and bitter but not salt and sugar, while van Cott et al. (1954) observed the opposite effect. Yamaguchi (1978) reported that the threshold of MSG did not increase substantially at high concentrations of other basic taste substances except sugar. These results conclusively show that the umami quality is not easily distinguishable in the presence of other …show more content…

Although palatable and savoury tastes develop when protein is hydrolysed into small peptides and amino acids, partial degradation produces bitterness which significantly decreases consumer acceptability of foods. The bitterness of protein hydrolysates has not been fully characterised and conflicting research is present, although it is predominantly attributed to the formation of bitter peptides rather than free amino acids (Sun, 2011). While L-enantiomers of higher molecular weight amino acids are bitter, Geisenhoff (2009) found that the bitterness of leucine and phenylalanine residues were perceived differently from enzyme-treated soy hydrolysate, suggesting free hydrophobic amino acids do not contribute to bitterness of soy protein hydrolysates. Intact proteins do not elicit bitter tastes as hydrophobic residues crucial for bitterness such as isoleucine, tyrosine, phenylalanine and tryptophan are orientated towards the interior of the three-dimensional structure and do not interact with taste receptors (Matoba & Hata, 1972). Upon hydrolysis, the protein structure is disrupted and hydrophobic residues are exposed to elucidate a bitter

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