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https://www.selleckchem.com/products/pf-04620110.html Research concerning the utilization of oilseed endogenous proteases is scarce. Herein, we investigated the peanut proteases and their effects on peanut proteins. Liquid chromatography tandem mass spectrometry analysis showed that peanut contained several endopeptidases and exopeptidases. Protease inhibitor assay and analysis of cleavage sites showed that the obvious proteolytic activity at pH 2-5 and 20-60 °C was from aspartic endopeptidases (optimal at pH 3) and one legumain (pH 4). The above endopeptidases destroyed five and six IgE-binding epitopes of Ara h 1 at pH 3 and 4, respectively. Ara h 1 (>95%) and arachin (50-60%) could be hydrolyzed to generate 10-20 kDa and less then 4 kDa peptides at pH 3, which was enhanced by the pH 3 → 4 incubation. Further, the limited hydrolysis improved the gel-forming ability and in vitro digestibility (approximately 15%) of peanut proteins. Free amino acid analysis showed that the activity of exopeptidases was low at pH 2-5.As a means of adding value, chicken foot broth byproduct can be processed to obtain calcium and bioactive peptides from the separated bones and meat residues. In this study, cleaned, dried, and powdered bones yielded 31.4 ± 0.6% calcium content. The meat residues were hydrolyzed to obtain over a hundred distinctive peptides, which were analyzed using LC-MS/MS and the SpirPep web-based tool. The peptides were rich in Glu, Asp, Lys, Gly and Leu, and also exhibited diverse bioactivities, among them primarily inhibition of dipeptidyl peptidase IV and angiotensin-converting enzyme. Calcium chelation assay determined the peptides to bind calcium at 235.7 ± 20.0 mg/g peptide-calcium chelate. Caco-2 cells treated with the chelate at calcium concentrations of 0-10 mM exhibited enhanced absorption relative to CaCl2. This demonstrates that calcium and chelating peptides generated from the same byproduct can produce peptide-calcium chelate, a potential ingredient in

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