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Related Experiment Videos

Bitter peptide from hemoglobin hydrolysate: isolation and characterization

I Aubes-Dufau1, J Capdevielle, J L Seris

  • 1INSA, Centre de Bioingénierie Gilbert Durand (URA CNRS 544), Toulouse, France.

FEBS Letters
|May 8, 1995
PubMed
Summary

A specific peptide, VV-hemorphin 7, is the primary cause of bitterness in peptic hemoglobin hydrolysates. This bitter peptide can be effectively detected and purified using hydrophobic adsorption chromatography.

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Area of Science:

  • Food Science
  • Biochemistry
  • Proteomics

Background:

  • Peptic hemoglobin hydrolysates are complex mixtures.
  • Bitterness is a significant sensory attribute affecting consumer acceptance.
  • Identifying the specific compounds responsible for bitterness is crucial for food processing.

Purpose of the Study:

  • To identify the major agent responsible for bitterness in peptic hemoglobin hydrolysates.
  • To develop an effective method for purifying the bitter peptide.
  • To characterize the bitter peptide and its sensory properties.

Main Methods:

  • Ultrafiltration and 2-butanol extraction were used for initial separation.
  • Hydrophobic adsorption on Superose 12 (gel-filtration) was employed for purification.

Related Experiment Videos

  • The bitter peptide was identified as VV-hemorphin 7, a fragment of bovine hemoglobin beta-chain.

    • Main Results:

    • A specific peptide was identified as the major contributor to bitterness.
    • Hydrophobic adsorption on Superose 12 proved effective for purification and bitterness detection.
    • VV-hemorphin 7 exhibited strong bitterness at 0.25 mM concentration.

    Conclusions:

    • VV-hemorphin 7 is the key bitter peptide in peptic hemoglobin hydrolysates.
    • Hydrophobic adsorption chromatography offers a novel method for bitterness detection and peptide purification.
    • Understanding the source of bitterness can guide strategies for improving food product quality.