BITTER PEPTIDE FROM HEMOGLOBIN HYDROLYSATE - ISOLATION AND CHARACTERIZATION

Citation
I. Aubesdufau et al., BITTER PEPTIDE FROM HEMOGLOBIN HYDROLYSATE - ISOLATION AND CHARACTERIZATION, FEBS letters, 364(2), 1995, pp. 115-119
Citations number
17
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
364
Issue
2
Year of publication
1995
Pages
115 - 119
Database
ISI
SICI code
0014-5793(1995)364:2<115:BPFHH->2.0.ZU;2-T
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 com plex 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 corresponde d to VV-hemorphin 7, the fragment 32-40 of the beta chain of bovine he moglobin, is first generated during proteolysis, then hydrolysed by pe psin, It exhibited a strong bitterness at 0.25 mM equivalent to 0.073 mM quinine sulfate or 21 mM caffeine.