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- W2040962313 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 β 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." @default.
- W2040962313 created "2016-06-24" @default.
- W2040962313 date "1995-05-08" @default.
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- W2040962313 title "Bitter peptide from hemoglobin hydrolysate: Isolation and characterization" @default.
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- W2040962313 doi "https://doi.org/10.1016/0014-5793(95)00361-c" @default.
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