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

Yu Fu; Kathrine Holmgaard Bak; Jing Liu; Cristian De Gobba; Marie Tøstesen; Erik T. Hansen; Mikael Agerlin Petersen; Jorge Ruiz Carrascal; Wender Bredie; Rene Lametsch

doi:10.1016/j.foodres.2019.03.017

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

Yu Fu, Kathrine Holmgaard Bak, Jing Liu, Cristian De Gobba, Marie Tøstesen, Erik T. Hansen, Mikael Agerlin Petersen, Jorge Ruiz Carrascal, Wender Bredie, Rene Lametsch^*

^*Corresponding author for this work

6 Citations (Scopus)

Abstract

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 language	English
Journal	Food Research International
Volume	121
Pages (from-to)	28-38
Number of pages	11
ISSN	0963-9969
DOIs	https://doi.org/10.1016/j.foodres.2019.03.017
Publication status	Published - 2019

Keywords

Blood
Exopeptidase
Hemoglobin
Protein hydrolysates
Taste
Volatile compounds

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10.1016/j.foodres.2019.03.017

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Fu, Y., Bak, K. H., Liu, J., De Gobba, C., Tøstesen, M., Hansen, E. T., Petersen, M. A., Ruiz Carrascal, J., Bredie, W., & Lametsch, R. (2019). Protein hydrolysates of porcine hemoglobin and blood: peptide characteristics in relation to taste attributes and formation of volatile compounds. Food Research International, 121, 28-38. https://doi.org/10.1016/j.foodres.2019.03.017

Fu, Y, Bak, KH, Liu, J , De Gobba, C, Tøstesen, M, Hansen, ET, Petersen, MA , Ruiz Carrascal, J , Bredie, W & Lametsch, R 2019, 'Protein hydrolysates of porcine hemoglobin and blood: peptide characteristics in relation to taste attributes and formation of volatile compounds', Food Research International, vol. 121, pp. 28-38. https://doi.org/10.1016/j.foodres.2019.03.017

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

abstract = "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.",

keywords = "Blood, Exopeptidase, Hemoglobin, Protein hydrolysates, Taste, Volatile compounds",

author = "Yu Fu and Bak, {Kathrine Holmgaard} and Jing Liu and {De Gobba}, Cristian and Marie T{\o}stesen and Hansen, {Erik T.} and Petersen, {Mikael Agerlin} and {Ruiz Carrascal}, Jorge and Wender Bredie and Rene Lametsch",

note = "(In Progress)",

year = "2019",

doi = "10.1016/j.foodres.2019.03.017",

language = "English",

volume = "121",

pages = "28--38",

journal = "Food Research International",

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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 -

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

Abstract

Keywords

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