作者: Kai Zhang , Jiawei Li , Hu Hou , Hongwei Zhang , Bafang Li
DOI: 10.1016/J.JFF.2018.11.042
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摘要: Abstract The calcium-binding peptides were recognized as novel functional ingredients for improving calcium bioavailability. Pacific cod (Gadus Macrocephalus) bone gelatin hydrolysates (BGH) with considerable binding activity (0.41 ± 0.08 μg/mg) prepared and then separated by hydroxyapatite specific affinity column chromatography reversed phase high performance liquid chromatography. A decapeptide was purified identified KGDPGLSPGK (designated Peptide-K, MW: 954.5 Da), which exhibited the highest (2.53 ± 0.12 μg/mg) among BGH. sites investigated circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR), mass spectrometry (MS). Results indicated that carboxylate O atoms of Asp-3 Lys-10 side chain amino N atom in Peptide-K contributed to calcium-chelating reaction. Possible chelating modes between Ca2+ constructed based on obtained data. may contribute a better understanding process peptides.