Metal solubility enhancing peptides derived from barley protein

被引:48
作者
Eckert, Ewelina [1 ]
Bamdad, Fatemeh [1 ]
Chen, Lingyun [1 ]
机构
[1] Univ Alberta, Dept Agr Food & Nutr Sci, Edmonton, AB T6G 2P5, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Barley protein hydrolysate; Metal binding; Enhanced metal solubility; Peptide structure; VITRO METHODS SOLUBILITY; CASEIN PHOSPHOPEPTIDES; BINDING PROPERTIES; CALCIUM; ZINC; BIOAVAILABILITY; ABSORPTION; DIALYZABILITY; TRANSPORT; DIGESTION;
D O I
10.1016/j.foodchem.2014.03.061
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Mineral supplements are required to be soluble as their bioavailability is highly correlated to their solubility in body fluids. In this study, metal binding capacity of barley protein hydrolysates and their purified fractions was investigated and expressed as increase in solubility of metal ions. Metal ions in the presence of hydrolysates exhibited a remarkable increase in solubility: 118, 32, 10, 29 and 35-fold for Fe2+, Fe3+, Ca2+, Cu2+ and Zn2+, respectively. A mixture of low molecular weight peptides possesses a synergistic combination of both charged and hydrophobic residues and achieves the best binding metal ions. Electrostatic interactions via charged side chains and coordination binding with His and Cys, initially attract the metal ions and, afterward, hydrophobic interactions and aromatic ring stacking stabilize the positioning of metal ions in the structure of the peptide. Barley hordein hydrolysates show potential as dietary supplements that enhance both mineral solubility and bioavailability. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:498 / 506
页数:9
相关论文
共 40 条
[1]   Antioxidant capacities of fractionated barley hordein hydrolysates in relation to peptide structures [J].
Bamdad, Fatemeh ;
Chen, Lingyun .
MOLECULAR NUTRITION & FOOD RESEARCH, 2013, 57 (03) :493-503
[2]   Effects of enzymatic hydrolysis on molecular structure and antioxidant activity of barley hordein [J].
Bamdad, Fatemeh ;
Wu, Jianping ;
Chen, Lingyun .
JOURNAL OF CEREAL SCIENCE, 2011, 54 (01) :20-28
[3]   Solubility and dissimilatory reduction kinetics of iron(III) oxyhydroxides: A linear free energy relationship [J].
Bonneville, Steeve ;
Behrends, Thilo ;
Van Cappellen, Philippe .
GEOCHIMICA ET COSMOCHIMICA ACTA, 2009, 73 (18) :5273-5282
[4]   Influence of various phosphopeptides of caseins on iron absorption [J].
Bouhallab, S ;
Cinga, V ;
Aít-Oukhatar, N ;
Bureau, F ;
Neuville, D ;
Arhan, P ;
Maubois, JL ;
Bouglé, D .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2002, 50 (24) :7127-7130
[5]   The osmotic pressure of electrostatically stabilized colloidal dispersions [J].
Bowen, WR ;
Williams, PM .
JOURNAL OF COLLOID AND INTERFACE SCIENCE, 1996, 184 (01) :241-250
[6]   Calcium absorption - A paradigm for mineral absorption [J].
Bronner, F .
JOURNAL OF NUTRITION, 1998, 128 (05) :917-920
[7]   Effectiveness of phosvitin peptides on enhancing bioavailability of calcium and its accumulation in bones [J].
Choi, I ;
Jung, C ;
Choi, H ;
Kim, C ;
Ha, H .
FOOD CHEMISTRY, 2005, 93 (04) :577-583
[8]   Enzymatic protein hydrolysates in human nutrition [J].
Clemente, A .
TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2000, 11 (07) :254-262
[9]  
Collins J.F., 2012, Physiology of the Gastrointestinal Tract, V1, P1921, DOI DOI 10.1016/B978-0-12-382026-6.00071-3
[10]   Casein phosphopeptides in oral health - Chemistry and clinical applications [J].
Cross, K. J. ;
Huq, N. L. ;
Reynolds, E. C. .
CURRENT PHARMACEUTICAL DESIGN, 2007, 13 (08) :793-800