Tilapia protein hydrolysate peptide was separated and purified by using zinc chelating polysaccharide affinity chromatography media. And the complexation reaction of peptide with zinc was investigated. The struc-ture characteristic of peptide-zinc complexes was characterized by HPLC, ICP-MS, UV-vis spectroscopy, FT-IR spectroscopy and SEM. The results showed that the tilapia hydrolysis polypeptide had been effectively purified and proved that chelating reaction between peptide and Zn2+had occurred and zinc-binding peptide complexes had been produced. The total zinc content of zinc-binding peptide complexes produced by hydrolysis polypeptide, TP1 and TP2 were 8.533%, 1.700%and 16.87%, respectively. The properties of zinc-peptide complexes was stable whose stability constant was 1.005×106.%采用自制的壳聚糖-Zn亲和层析介质对罗非鱼蛋白多肽进行分离纯化,筛选出与Zn2+有较强配位作用的亲和肽,并研究Zn2+与亲和肽的配位作用动力学及形成配合物的结构特征.采用高效液相色谱、电感耦合等离子体质谱(ICP-MS)、紫外及红外光谱仪、扫描电子显微镜等分析手段对肽-锌配合物进行结构表征.结果表明,制备的壳聚糖-Zn亲和介质能够实现从罗非鱼蛋白酶解产物中选择性筛选分离出与Zn2+有较强配位作用的亲和肽;多肽原液、TP1组分、TP2组分与Zn2+通过配合反应形成肽-锌配合物的锌含量分别为8.533%、1.700%、16.87%;所得亲和肽与Zn2+具有较强配位作用,配合物的稳定常数为1.005×106,并分析了肽-锌配合物的基本结构特征.
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