Calcium is one of the most important mineral elements in the human body and is closely related to the maintenance of human health. To prevent calcium deficiency, various calcium supplements have been developed, but their application tends to be limited by low calcium content and highly irritating effects on the stomach, among other side effects. Recently, calcium–peptide chelates, which have excellent stability and are easily absorbed, have received attention as an alternative emerging calcium supplement. Calcium-binding peptides (CaBP) are usually obtained via the hydrolysis of animal or plant proteins, and calcium-binding capacity (CaBC) can be further improved through chromatographic purification techniques. In calcium ions, the phosphate group, carboxylic group and nitrogen atom in the peptide are the main binding sites, and the four modes of combination are the unidentate mode, bidentate mode, bridging mode and α mode. The stability and safety of calcium–peptide chelates are discussed in this paper, the intestinal absorption pathways of calcium elements and peptides are described, and the bioavailability of calcium–peptide chelates, both in vitro and in vivo, is also introduced. This review of the research status of calcium–peptide chelates aims to provide a reasonable theoretical basis for their application as calcium supplementation products.
Soybean trypsin inhibitor (STI) was obtained from simulated soybean whey wastewater through a sustainable method consisting of isoelectric precipitation, ammonium sulfate salting out, and gel filtration chromatography, and the effect of temperature, pH, and pepsin on the stability of STI was also discussed. The results showed that the recovery rate of the trypsin inhibitory activity was 89.47%, the purity and the specific activity of STI were 71.11%, and 1442.5 TIU/mg in the conditions of pH 4.0 and 40% ammonium sulfate saturation. The soybean Kunitz trypsin inhibitor (KTI) and soybean Bowman–Brik trypsin inhibitor (BBI) were obtained via gel filtration chromatography, and their specific activity levels were 1733.5 TIU/mg and 2588.3 TIU/mg, respectively. The STI displayed good stability over a wide temperature and pH range. The STI, KTI, and BBI were all resistant to pepsin hydrolysis, and their ability was ranked as BBI > STI > KTI. These findings will provide a theoretical basis for recycling STI from soybean whey wastewater and promoting better active compound utilization.
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