Exopeptidase treatment combined with Maillard reaction modification of protein hydrolysates derived from porcine muscle and plasma: structure–taste relationship
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Exopeptidase treatment combined with Maillard reaction modification of protein hydrolysates derived from porcine muscle and plasma : structure–taste relationship. / Fu, Yu; Liu, Jing; Zhang, Wei; Wæhrens, Sandra S.; Tøstesen, Marie; Hansen, Erik T.; Bredie, Wender L. P.; Lametsch, Rene.
In: Food Chemistry, Vol. 306, 125613, 2020.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Exopeptidase treatment combined with Maillard reaction modification of protein hydrolysates derived from porcine muscle and plasma
T2 - structure–taste relationship
AU - Fu, Yu
AU - Liu, Jing
AU - Zhang, Wei
AU - Wæhrens, Sandra S.
AU - Tøstesen, Marie
AU - Hansen, Erik T.
AU - Bredie, Wender L. P.
AU - Lametsch, Rene
PY - 2020
Y1 - 2020
N2 - Reduction of bitter taste in protein hydrolysates is a challenging task. The aim of this study was to apply a simple two-step approach to prepare low bitter hydrolysates and investigate the influence of peptide modifications on taste characteristics. Protein hydrolysates were prepared from porcine muscle and plasma through simultaneous hydrolysis using endo- and exo-peptidases combined with peptide glycation by glucosamine (GlcN). Spectroscopic analysis and quantification of major alpha-dicarbonyl compounds (α-DCs) indicated the relatively low extent of Maillard reaction in GlcN-glycated protein hydrolysates. Thermal degradation of high MW peptides (>10 kDa) might play a major role in Maillard reaction, reflected by the formation of more Maillard reacted peptides (1–5 kDa), especially in plasma samples. Sensory evaluation indicated that glycation by GlcN can alter taste profiles of protein hydrolysates, which may be attributed to the formation of Maillard reacted peptides and peptide modifications revealed by LC–MS/MS analysis.
AB - Reduction of bitter taste in protein hydrolysates is a challenging task. The aim of this study was to apply a simple two-step approach to prepare low bitter hydrolysates and investigate the influence of peptide modifications on taste characteristics. Protein hydrolysates were prepared from porcine muscle and plasma through simultaneous hydrolysis using endo- and exo-peptidases combined with peptide glycation by glucosamine (GlcN). Spectroscopic analysis and quantification of major alpha-dicarbonyl compounds (α-DCs) indicated the relatively low extent of Maillard reaction in GlcN-glycated protein hydrolysates. Thermal degradation of high MW peptides (>10 kDa) might play a major role in Maillard reaction, reflected by the formation of more Maillard reacted peptides (1–5 kDa), especially in plasma samples. Sensory evaluation indicated that glycation by GlcN can alter taste profiles of protein hydrolysates, which may be attributed to the formation of Maillard reacted peptides and peptide modifications revealed by LC–MS/MS analysis.
KW - Bitterness
KW - Exopeptidase
KW - Glucosamine
KW - Maillard reaction
KW - Protein hydrolysates
KW - α-Dicarbonyl compounds
U2 - 10.1016/j.foodchem.2019.125613
DO - 10.1016/j.foodchem.2019.125613
M3 - Journal article
C2 - 31610331
AN - SCOPUS:85073028178
VL - 306
JO - Food Chemistry
JF - Food Chemistry
SN - 0308-8146
M1 - 125613
ER -
ID: 230895572