Exopeptidase treatment combined with Maillard reaction modification of protein hydrolysates derived from porcine muscle and plasma: structure–taste relationship

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

SN - 0308-8146

VL - 306

JO - Food Chemistry

JF - Food Chemistry

M1 - 125613

ER -