Protein hydrolysates of porcine hemoglobin and blood: peptide characteristics in relation to taste attributes and formation of volatile compounds
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Protein hydrolysates of porcine hemoglobin and blood : peptide characteristics in relation to taste attributes and formation of volatile compounds. / Fu, Yu; Bak, Kathrine Holmgaard; Liu, Jing; De Gobba, Cristian; Tøstesen, Marie; Hansen, Erik T.; Petersen, Mikael Agerlin; Ruiz Carrascal, Jorge; Bredie, Wender; Lametsch, Rene.
In: Food Research International, Vol. 121, 2019, p. 28-38.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
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
VL - 121
SP - 28
EP - 38
JO - Food Research International
JF - Food Research International
SN - 0963-9969
ER -
ID: 215361264