Gallic acid oxidizes Met residues in peptides released from bovine β-lactoglobulin by in vitro digestion

Ping Lai, Atsushi Okazawa, Yoshihiro Izumi, Takeshi Bamba, Eiichiro Fukusaki, Masaaki Yoshikawa, Akio Kobayashi

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)297-305
Number of pages9
JournalJournal of Bioscience and Bioengineering
Volume114
Issue number3
DOIs
Publication statusPublished - Sep 1 2012
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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