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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.