title: Bitter peptide from hemoglobin hydrolysate: isolation and characterization.
abstract: Two separation methods, ultrafiltration and 2-butanol extraction, have shown that a peptide is the major agent responsible for bitterness in peptic hemoglobin hydrolysates. It was easily purified from these complex mixtures by specific hydrophobic adsorption on Superose 12, a gel-filtration column, which could constitute an original and interesting method for bitterness detection. The bitter peptide which corresponded to VV-hemorphin 7, the fragment 32-40 of the beta chain of bovine hemoglobin, is first generated during proteolysis, then hydrolysed by pepsin. It exhibited a strong bitterness at 0.25 mM equivalent to 0.073 mM quinine sulfate or 21 mM caffeine.
authors.affiliation: INSA, Centre de Bioingénierie Gilbert Durand (URA CNRS 544), Toulouse, France.
authors.forename: I
authors.initials: I
authors.lastname: Aubes-Dufau
authors.forename: J
authors.initials: J
authors.lastname: Capdevielle
authors.forename: J L
authors.initials: JL
authors.lastname: Seris
authors.forename: D
authors.initials: D
authors.lastname: Combes
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D005504:Food Analysis; D006454:Hemoglobins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D013649:Taste
chemical_list: D006454:Hemoglobins; D010455:Peptides