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

被引：3

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

来源：

JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2012年 / 114卷 / 03期

关键词：

Gallic acid; beta-Lactoglobulin; Liquid chromatography/ion trap-time of flight-mass spectrometry (LC/IT-TOF-MS); Methionine sulfoxide; Trypsin digestion; PHENOLIC-COMPOUNDS; ANTIOXIDANT; HYDROLYSIS; METHIONINE; OXIDATION; PROTEINS; IDENTIFICATION; POLYPHENOLS; RESISTANCE; APOPTOSIS;

D O I：

10.1016/j.jbiosc.2012.04.019

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：

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 beta-lactoglobulin (beta-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 beta-LG digestion. However, after 1.5 h of digestion, the observed degree of hydrolysis of beta-LG was lower in the presence than in the absence of GA. The peptides released from beta-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 beta-LG in the presence of GA. Met(7), Met(24) and Met(145) in the peptides corresponding to these peaks were oxidized to methionine sulfoxide residues. (C) 2012, The Society for Biotechnology, Japan. All rights reserved.

引用

页码：297 / 305

页数：9

共 31 条

[1] DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].

ADLERNISSEN, J .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1979, 27 (06) :1256-1262

[2] Production of hydrogen peroxide by polyphenols and polyphenol-rich beverages under quasi-physiological conditions [J].

Akagawa, M ;

Shigemitsu, T ;

Suyama, K .

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 2003, 67 (12) :2632-2640

[3] CHYMOTRYPSIN - MOLECULAR AND CATALYTIC PROPERTIES [J].

APPEL, W .

CLINICAL BIOCHEMISTRY, 1986, 19 (06) :317-322

[4]

Arts ICW, 2005, AM J CLIN NUTR, V81, p317S, DOI 10.1093/ajcn/81.1.317S

[5] EVALUATION OF THE ANTIOXIDANT AND PROOXIDANT ACTIONS OF GALLIC ACID AND ITS DERIVATIVES [J].

ARUOMA, OI ;

MURCIA, A ;

BUTLER, J ;

HALLIWELL, B .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1993, 41 (11) :1880-1885

[6] Phenolic compounds in plants and agri-industrial by-products: Antioxidant activity, occurrence, and potential uses [J].

Balasundram, Nagendran ;

Sundram, Kalyana ;

Samman, Samir .

FOOD CHEMISTRY, 2006, 99 (01) :191-203

[7] BETA-LACTOGLOBULINS [J].

BELL, K ;

MCKENZIE, HA .

NATURE, 1964, 204 (496) :1275-&

[8]

BRUNE M, 1989, EUR J CLIN NUTR, V43, P547

[9] Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of β-lactoglobulin: Analysis by LC-ESI-TOF/MS [J].

Cheison, Seronei Chelulei ;

Schmitt, Meike ;

Leeb, Elena ;

Letzel, Thomas ;

Kulozik, Ulrich .

FOOD CHEMISTRY, 2010, 121 (02) :457-467

[10] SECONDARY STRUCTURE OF BOVINE BETA-LACTOGLOBULIN-B [J].

CREAMER, LK ;

PARRY, DAD ;

MALCOLM, GN .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1983, 227 (01) :98-105

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