PROTEIN-PHYTATE INTERACTIONS IN SOYBEANS. II. MECHANISM OF PROTEIN-PHYTATE BINDING AS AFFECTED BY CALCIUM

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Abstract
Phytate and bovine serum albumin were used in a model system to investigate the mechanism of their binding. Ultrafiltration studies using response surface design showed the association of protein and phytic acid to be highly pH dependent. Under acid conditions, the protein formed an insoluble complex with phytic acid. At pH 3.0, a binding constant of 2.3 times 105 was obtained and it was calculated that there are 78 binding sites of the total 93 basic amino acid residues potentially available. This low pH complex was not disrupted at high temperatures but the presence of calcium ions caused dissolution of the precipitate. Calcium produced different effects at higher pH (> 6). Soluble protein-calcium-phytic acid complexes were formed which were less stable to heat and dissociated above pH 10 at high ionic strength. Since this interaction occurred only in the presence of calcium, a salt linkage is implicated in which divalent cations simultaneously bind to the protein and phytic acid in the form of a soluble complex. It is proposed that either the addition of divalent cations at low pH or sequestering agents at high pH would best effect the removal of phytate from soy products by ultrafiltration.

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