Protein hydrolysates of porcine hemoglobin and blood: peptide characteristics in relation to taste attributes and formation of volatile compounds

Research output: Contribution to journalJournal article

The objective of this study was to investigate the impact of endo- and exo-peptidase treatment on certain structural characteristics of peptides and volatile compounds of porcine hemoglobin and whole blood hydrolysates. Porcine hemoglobin and whole blood were hydrolyzed by endo- and exo-peptidases. The presence of exopeptidases reduced the bitterness and altered the volatile profiles of protein hydrolysates. Exopeptidase treatment can release terminal amino acids from peptides, which in turn may contribute to formation of volatile compounds by Maillard reactions. In contrast, endopeptidases conferred a slightly bitter taste and different volatile profiles. For hemoglobin hydrolysates, principal component analysis revealed that proteases were categorized into three groups based on endo- or exo-peptidase activity. Whole blood is a more complex raw material, yet the proteases were still categorized in a similar fashion. This work contributes to understanding structural characteristics responsible for taste and volatile profiles of protein hydrolysates.

Original languageEnglish
JournalFood Research International
Volume121
Pages (from-to)28-38
Number of pages11
ISSN0963-9969
DOIs
Publication statusPublished - 2019

    Research areas

  • Blood, Exopeptidase, Hemoglobin, Protein hydrolysates, Taste, Volatile compounds

ID: 215361264