Abstract
SummaryHydrolysed proteins from sunflower seed and peanut were separated by ultrafiltration. Results showed that 1–3 kDa sunflower seed peptide (SSP4) and ≥10 kDa peanut peptide (PP1) fractions had the highest Ca‐binding capacity of 104.80 and 124.74 mg g−1, respectively. After Ca binding, scanning electron microscopy results showed that the loose sheet‐like structure of SSP4 and PP1 transformed into a granular structure. Fourier‐transform infrared spectroscopy results showed that carboxyl and amide groups were involved in Ca binding. Growing male mice were assigned to eight groups: control, CaCO3 and six experimental groups (low, medium and high doses for each SSP4‐Ca and PP1‐Ca). Apparent Ca absorption rate, bone mineral density (BMD), bone surface microstructure and biomechanical index and serum biochemical index were evaluated. Animal experiment results indicated that SSP4‐Ca and PP1‐Ca can improve Ca bioavailability; effectively enhance BMD and structure; and promote Ca absorption. The peptide–Ca complexes were absorbed better than CaCO3 and promoted Ca accumulation in the bone. PP1‐Ca was better than SSP4‐Ca in promoting calcium absorption and enhancing BMD.
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