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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Novel Peptide with a Specific Calcium-Binding Capacity from Whey Protein Hydrolysate and the Possible Chelating Mode
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Novel Peptide with a Specific Calcium-Binding Capacity from Whey Protein Hydrolysate and the Possible Chelating Mode

机译：乳清蛋白水解物中具有特定钙结合能力的新型肽及其可能的螯合模式

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摘要

A novel peptide with a specific calcium-binding capacity was isolated from whey protein hydrolysates. The isolation procedures included diethylaminoethyl (DEAE) anion-exchange chromatography, Sephadex G-25 gel filtration, and reversed-phase high-performance liquid chromatography (HPLC). A peptide with a molecular mass of 237.99 Da was identified by liquid chromatography—electrospray ionization/mass spectrometry (LC—ESI/MS), and its amino acid sequence was confirmed to be Gly-Tyr. The calcium-binding capacity of Gly-Tyr reached 75.38 μg/mg, increasing by 122% when compared to the hydrolysate complex. The chelating interaction mode between the Gly-Tyr and calcium ion was investigated, indicating that the major binding sites included the oxygen atom of the carbonyl group and nitrogen of the amino or imino group. The folding and structural modification of the peptide arose along with the addition of the calcium ion. The profile of ~1H nuclear magnetic resonance (NMR) spectroscopy demonstrated that the electron cloud density around the hydrogen nucleus in the peptide changed was caused by the calcium ion. The results of ζ potential showed that the Gly-Tyr—Ca chelate was a neutral molecule in which the calcium ion was surrounded by the specific binding sites of the peptide. Moreover, thermogravimetry—differential scanning calorimetry (TG-DSC) and calc ium-releasing assay revealed that the Gly-Tyr—Ca chelate exerted excellent thermal stability and solubility in both acidic and basic conditions, which were beneficial to calcium absorption in the gastrointestinal tract of the human body and, therefore, improved its bioavailability. These findings further the progress in the research of whey protein, suggesting the potential in making peptide—calcium chelate as a dietary supplement.
机译：从乳清蛋白水解物中分离出具有特定钙结合能力的新型肽。分离步骤包括二乙氨基乙基（DEAE）阴离子交换色谱，Sephadex G-25凝胶过滤和反相高效液相色谱（HPLC）。通过液相色谱-电喷雾电离/质谱（LC-ESI / MS）鉴定了分子量为237.99Da的肽，并确认其氨基酸序列为Gly-Tyr。与水解产物复合物相比，Gly-Tyr的钙结合能力达到75.38μg/ mg，增加了122％。研究了Gly-Tyr与钙离子之间的螯合相互作用模式，表明主要的结合位点包括羰基的氧原子和氨基或亚氨基的氮。肽的折叠和结构修饰与钙离子的添加​​一起出现。 〜1H核磁共振（NMR）谱图表明，肽中氢核周围电子云密度的变化是由钙离子引起的。 ζ电势的结果表明，Gly-Tyr-Ca螯合物是中性分子，其中钙离子被肽的特异性结合位点包围。此外，热重分析-差示扫描量热法（TG-DSC）和钙释放分析表明，Gly-Tyr-Ca螯合物在酸性和碱性条件下均具有优异的热稳定性和溶解性，这有利于胃肠道中钙的吸收。从而改善其生物利用度。这些发现进一步促进了乳清蛋白的研究进展，表明了将肽螯合钙制成膳食补充剂的潜力。

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