TY - JOUR
T1 - Gallic acid oxidizes Met residues in peptides released from bovine β-lactoglobulin by in vitro digestion
AU - Lai, Ping
AU - Okazawa, Atsushi
AU - Izumi, Yoshihiro
AU - Bamba, Takeshi
AU - Fukusaki, Eiichiro
AU - Yoshikawa, Masaaki
AU - Kobayashi, Akio
N1 - Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2012/9
Y1 - 2012/9
N2 - Phenolic compounds (PCs) are frequently present in foods. However, little is known about the effect of PCs on enzymatic digestion process of food proteins and their products. In this study, the effect of gallic acid (GA) on in vitro digestion of β-lactoglobulin (β-LG) was investigated as a model system for analysis of the interaction between PCs and food proteins. GA showed no effect on the initial rate of β-LG digestion. However, after 1.5 h of digestion, the observed degree of hydrolysis of β-LG was lower in the presence than in the absence of GA. The peptides released from β-LG were characterized by LC/IT-TOF-MS and thirty peptides were identified. In particular, four new peaks were obtained following in vitro digestion of β-LG in the presence of GA. Met7, Met24 and Met145 in the peptides corresponding to these peaks were oxidized to methionine sulfoxide residues.
AB - Phenolic compounds (PCs) are frequently present in foods. However, little is known about the effect of PCs on enzymatic digestion process of food proteins and their products. In this study, the effect of gallic acid (GA) on in vitro digestion of β-lactoglobulin (β-LG) was investigated as a model system for analysis of the interaction between PCs and food proteins. GA showed no effect on the initial rate of β-LG digestion. However, after 1.5 h of digestion, the observed degree of hydrolysis of β-LG was lower in the presence than in the absence of GA. The peptides released from β-LG were characterized by LC/IT-TOF-MS and thirty peptides were identified. In particular, four new peaks were obtained following in vitro digestion of β-LG in the presence of GA. Met7, Met24 and Met145 in the peptides corresponding to these peaks were oxidized to methionine sulfoxide residues.
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U2 - 10.1016/j.jbiosc.2012.04.019
DO - 10.1016/j.jbiosc.2012.04.019
M3 - Article
C2 - 22652084
AN - SCOPUS:84864606620
SN - 1389-1723
VL - 114
SP - 297
EP - 305
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 3
ER -