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Taste modification of amino acids and protein hydrolysate by α-cyclodextrin
- Linde, Giani Andrea, Laverde Junior, Antonio, Faria, Eliete Vaz de, Colauto, Nelson Barros, Moraes, Flavio Faria de, Zanin, Gisella Maria
- Food research international 2009 v.42 no.7 pp. 814-818
- cyclodextrins, protein hydrolysates, amino acids, soy protein, pH, phenylalanine, tyrosine, isoleucine, proline, histidine, amino acid composition, nuclear magnetic resonance spectroscopy, sensory evaluation, taste, bitterness, beverage industry
- The objective of this work was to characterize the formation of amino acid inclusion complexes with α-cyclodextrin (α-CD) and evaluate the influence of added α-CD on the taste perception of amino acids and hydrolyzed soy protein at pH 4.5. The formation of the inclusion complexes of phenylalanine, tryptophane, tyrosine, isoleucine, proline and histidine with α-CD were detected by nuclear magnetic resonance techniques (ROESY and DOSY) and the sensory characteristics of soy hydrolysates were judged by a panel of trained tasters. It was concluded that these amino acids form inclusion complexes with α-CD and the order of affinity for the α-CD cavity is phenylalanine approximately equal to tryptophane > proline > isoleucine approximately equal to tyrosine approximately equal to histidine. α-CD alters the bitter taste perception of the amino acids and reduces the bitter taste from hydrolyzed soy protein. These results indicate a potential use of α-CD for debittering protein hydrolysates in acidic beverages.