Effect of extraction method on the calcium binding capacity of faba bean globulin fractions at various pH

Faba bean ingredients are rich in proteins and good sources of calcium (Ca), although containing phytic acid (PA) molecules. PA, a polyphosphate compound, can affect the bioavailability of minerals/proteins through complex formation. This study evaluates the impact of two extraction processes, Alkaline Extraction-IsoElectric Precipitation (AE-IEP) and Sequential Extraction (SE), on the ability of faba bean globulin systems to bind added calcium ions. Increasing concentrations of CaCl2 were introduced into 2.5% (w/v) protein dispersions at pHs 4.5, 5.5, 6.5, and 7.5, and free Ca monitored. Near the isoelectric point of globulin (pH ∼ 4–5), Ca binding capacity was found to be low. At higher pHs, significant Ca chelation occurred, initially attributed to free PA binding sites, resulting in the formation of insoluble complexes and subsequent protein precipitation. The AE-IEP globulin fraction exhibited a higher Ca binding capacity than the SE globulin, attributed to its higher PA and lower initial Ca concentrations. •AE-IEP globulins are richer in PA and contain lower amount of Ca than SE globulins.•Ca binding capacity is high at pHs 6.5/7.5 but lower close to globulin pI.•High pH values induce Ca/globulin complex formation and protein precipitation.•AE-IEP globulins have greater ability to bind calcium compared to SE globulins.