2014
DOI: 10.1016/j.foodchem.2014.03.061
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Metal solubility enhancing peptides derived from barley protein

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Cited by 43 publications
(39 citation statements)
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“…It is reported that hydrolysates can exert binding activity towards different minerals such as calcium , Huang et al, 2011, iron (Chaud et al, 2002;Lee and Song, 2009a), copper (Eckert et al, 2014), and zinc (Eckert et al, 2014). Different molecular sizes of the mineral binding peptides ranging from 1 to 1.5 kDa have been reported ( …”
Section: Mineral Bindingmentioning
confidence: 99%
“…It is reported that hydrolysates can exert binding activity towards different minerals such as calcium , Huang et al, 2011, iron (Chaud et al, 2002;Lee and Song, 2009a), copper (Eckert et al, 2014), and zinc (Eckert et al, 2014). Different molecular sizes of the mineral binding peptides ranging from 1 to 1.5 kDa have been reported ( …”
Section: Mineral Bindingmentioning
confidence: 99%
“…The solubility of the peptide fractions-zinc complexes was determined according to the literature with some modifications [16]. Diverse pH conditions were generated using appropriate buffers at 0.1 mol/L (KCl-HCl and citric acid phosphate buffer solution).…”
Section: Zinc Solubility In Various Ph Valuesmentioning
confidence: 99%
“…Furthermore, the molecular weight of hydrolysate fraction decreases with the increase of DH under certain hydrolysis conditions and it indicated that low molecular weight peptide fraction with higher DH exhibited the higher surface charge. The surface charge of the peptides was conducive to the stability of the particles except when the particle size could not be balanced with electrostatic repulsion [16,21,22]. The low molecular weight peptide fraction P1 exhibited the strong zinc chelation capacity, this can be due to the high electrostatic repulsion at P1 surface, reflected by high magnitude zeta potential, which inhibit intermolecular aggregation leading to small peptide particles.…”
Section: Zeta Potential Of the Peptide Fractionsmentioning
confidence: 99%
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“…() highlighted the importance of this requirement. The affinity for binding between the protein (or peptide) and the mineral must be able to protect the mineral during the initial stages of digestion but also be low enough to allow for suitable release in the lower digestive tract (jejunum and duodenum) (Eckert, Bamdad, & Chen, ). While it has been suggested that unique transcellular pathway(s) may be available for some chelated minerals, none of these pathways have yet been identified or characterized (Cosentino et al., ; Hou et al., ).…”
Section: Minerals Present In Milk and Dairy Productsmentioning
confidence: 99%