Effect of gallic acid on peptides released by trypsin digestion of bovine α-casein

被引:1
作者
Lai, Ping [1 ]
Okazawa, Atsushi [1 ,2 ]
Izumi, Yoshihiro [1 ]
Bamba, Takeshi [1 ]
Fukusaki, Eiichiro [1 ]
Yoshikawa, Masaaki [3 ]
Kobayashi, Akio [1 ]
机构
[1] Osaka Univ, Grad Sch Engn, Dept Biotechnol, Suita, Osaka 5650871, Japan
[2] Osaka Prefecture Univ, Grad Sch Life & Environm Sci, Dept Appl Life Sci, Naka Ku, Sakai, Osaka 5998531, Japan
[3] Res Inst Prod Dev, Sakyo Ku, Kyoto 6060805, Japan
关键词
Angiotensin I-converting enzyme inhibitory activity; alpha-Casein; Gallic acid; Liquid chromatography/ion-trap time-of-flight mass spectrometry (LC/IT-TOF-MS); Methionine sulfoxide; Trypsin digestion; PHENOLIC-COMPOUNDS; CONVERTING-ENZYME; ANTIOXIDANT; PROTEINS; HYDROLYSIS; RESIDUES;
D O I
10.1016/j.jbiosc.2012.10.003
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
In this study, the effects of gallic acid (GA) on trypsin digestion of commercial alpha-casein (alpha-CN), which contains alpha(s1)-CN and alpha(s2)-CN, and the peptides released during digestion were investigated. Gallic acid showed no effect on the initial rate of digestion. However, the apparent degree of hydrolysis achieved its maximum value after 1 h, then decreased in the presence of GA, suggesting the cross-linking between peptides once released from alpha-CN during digestion. In the presence of GA, three peaks derived from alpha(s1)-CN disappeared and three new peaks appeared in high-performance liquid chromatography (HPLC) analysis. In these peptides, two Met residues corresponding to the Met(135) and Met(196) in alpha(s1)-CN were oxidized to Met sulfoxide residues. The oxidation of Met(196) was quicker than that of Met(135). The inhibitory activity of TTMPLW (alpha(s1)-CN 193-199) against angiotensin I-converting enzyme was reduced slightly by the oxidation of its Met residue. (C) 2012, The Society for Biotechnology, Japan. All rights reserved.
引用
收藏
页码:259 / 267
页数:9
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