Portal de Periódicos da CAPES

Artigo Acesso aberto Produção Nacional Revisado por pares

BIBTEX RIS

Taste modification of amino acids and protein hydrolysate by α-cyclodextrin

2009; Elsevier BV; Volume: 42; Issue: 7 Linguagem: Inglês

10.1016/j.foodres.2009.03.016

1873-7145

Giani Andréa Linde, Antônio Laverde, Eliete Vaz de Faria, Nelson Barros Colauto, Flávio Faria de Moraes, Gisella Maria Zanin,

Protein Hydrolysis and Bioactive Peptides

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 ≈ tryptophane > proline > isoleucine ≈ tyrosine ≈ 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.