A novel calcium-chelating peptide purified from Auxis thazard protien hydrolysate and its binding properties with calcium
A novel calcium-chelating peptide purified from Auxis thazard protien hydrolysate and its binding properties with calcium
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DOI：
10.1016/j.jff.2019.103447
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发表时间：
2019-09-01
影响因子：
5.6
通讯作者：
Liu, Shucheng
中科院分区：
文献类型：
--
作者：
Chen, Ming;Ji, Hongwu;Liu, Shucheng
采用酶解和膜分离的方法制备了萨扎德蛋白肽，并根据其钙离子结合能力，采用Sephadex G-15凝胶层析和反相高效液相色谱（RP-HPLC）对萨扎德蛋白肽进行了纯化。从Auxis thazard蛋白肽中纯化得到一种新的钙结合活性最高的肽（76.8 ± 4.5 mg/g），经鉴定为Glu-Pro-Ala-His（分子量为453.3 Da）。红外光谱和质谱分析结果表明，钙结合肽的结合位点既包括谷氨酸的羧基，也包括组氨酸的羧基和氨基。构建了肽钙螯合物的分子模型，并通过扫描电镜证实了肽（Glu-Pro-Ala-His）与钙螯合前后分子结构和表观结构的差异。这些研究结果表明，Auxis thazard蛋白水解物是一种高质量的具有钙结合活性的肽源。
Auxis thazard protein peptides were prepared by enzymatic hydrolysis and membrane separation and then sequentially purified with Sephadex G-15 gel chromatography and reversed phase high performance liquid chromatography (RP-HPLC) based on their calcium binding capacity. A novel peptide purified from Auxis thazard protien peptides exhibited the highest calcium binding activity (76.8 +/- 4.5 mg/g) and was identified as Glu-Pro-Ala-His (MW = 453.3 Da). The results of FTIR and mass spectrometry showed that the binding sites of calcium-binding peptide involved the carboxylic group of Glu, as well as the carboxylic group and the amino group of His. A hypothesized molecular model of peptide-calcium chelate was constructed and the difference of the molecular structure and apparent structure of peptide (Glu-Pro-Ala-His) before and after chelating with calcium was also confirmed by scanning electron microscope. These study results indicated that Auxis thazard protein hydrolysate was a high quality source of peptides with calcium binding activity.