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

TY - JOUR

T1 - Protein hydrolysates of porcine hemoglobin and blood

T2 - peptide characteristics in relation to taste attributes and formation of volatile compounds

AU - Fu, Yu

AU - Bak, Kathrine Holmgaard

AU - Liu, Jing

AU - De Gobba, Cristian

AU - Tøstesen, Marie

AU - Hansen, Erik T.

AU - Petersen, Mikael Agerlin

AU - Ruiz Carrascal, Jorge

AU - Bredie, Wender

AU - Lametsch, Rene

N1 - (In Progress)

PY - 2019

Y1 - 2019

N2 - 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.

AB - 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.

KW - Blood

KW - Exopeptidase

KW - Hemoglobin

KW - Protein hydrolysates

KW - Taste

KW - Volatile compounds

U2 - 10.1016/j.foodres.2019.03.017

DO - 10.1016/j.foodres.2019.03.017

M3 - Journal article

C2 - 31108750

AN - SCOPUS:85062872912

SN - 0963-9969

VL - 121

SP - 28

EP - 38

JO - Food Research International

JF - Food Research International

ER -