4.7 Article

Molecular Characterization of Whey Protein Hydrolysate Fractions with Ferrous Chelating and Enhanced Iron Solubility Capabilities

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 63, Issue 10, Pages 2708-2714

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf505817a

Keywords

whey protein; enzymatic hydrolysis; iron-binding; Simulated digestion; FTIR

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The ferrous (Fe2+) chelating capabilities of WPI hydrolysate fractions produced via cascade membrane filtration were investigated, specifically 1 kDa permeate (P) and 30 kDa retentate (R) fractions. The 1 kDa-P possessed a Fe2+ chelating capability at 1 g L-1 equivalent to 84.4 mu M EDTA (for 30 kDa-R the value was 8.7 mu M EDTA). Fourier transformed infrared (FTIR) spectroscopy was utilized to investigate the structural characteristics of hydrolysates and molecular interactions with Fe2+. Solid-phase extraction was employed to enrich for chelating activity; the most potent chelating fraction was enriched in histidine and lysine. The solubility of ferrous sulfate solutions (10 mM) over a range of pH values was significantly (P < 0.05) improved in dispersions of hydrolysate fraction solutions (10 g protein L-1). Total iron solubility was improved by 72% in the presence of the 1 kDa-P fraction following simulated gastrointestinal digestion (SGID) compared to control FeSO4.7H(2)O solutions.

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