乌鸡低聚肽亚铁螯合物的分离纯化与结构鉴定

Isolation and Structural Identification of Iron (II)-Chelated Oligopeptides from Black-Bone Silky Fowl

摘要:

从乌鸡中酶解得到乌鸡低聚肽，然后与亚铁螯合制备乌鸡低聚肽亚铁螯合物，螯合率为84.76±0.12%。乌鸡低聚肽亚铁螯合物具有较高的蛋白质含量，高达54.64±1.03%。并且分子量较低，其中分子量小于1000 u的占85.50%。通过扫描电镜、红外光谱对乌鸡低聚肽亚铁螯合物的结构进行分析，结果表明乌鸡低聚肽亚铁螯合物是一种新型的铁螯合物。体外稳定性研究表明乌鸡低聚肽亚铁螯合物具有一定的热稳定性、酸碱稳定性和体外消化稳定性。通过反相高效液相色谱对乌鸡低聚肽亚铁螯合物进行分离纯化，选择一个主要的组分进行收集，然后利用质谱仪进行质谱分析。从乌鸡低聚肽亚铁螯合物的主要组分中鉴定出一个五肽，氨基酸序列为Thr-Ser-Gly-Met-Pro。乌鸡低聚肽亚铁螯合物可作为一种铁补充剂用于食品添加剂、营养物及医药制品中。

Abstract:

Black-bone silky fowl oligopeptides (BSFOP) were prepared by enzymatic hydrolysis of muscle from black-bone silky fowls and then reacted with iron (II) to yield iron (II)-chelated black-bone silky fowl oligopeptides (BSFOP-Fe). The iron-chelating capacity of BSFOP was 84.76±0.12%. BSFOP-Fe had a high protein content (54.64 ± 1.03%) and low molecular weight; 85.50% of peptides were less than 1000 u. Scanning electron microscopy, ultraviolet (UV) wavelength scanning, and infrared spectra were used to analyze the structure of BSFOP-Fe, and the results showed that BSFOP-Fe was a new type of iron-chelated compound. An in vitro stability study indicated that BSFOP-Fe maintained certain stability against temperature, pH, and in vitro gastric protease digestion. BSFOP-Fe was separated and purified by reverse-phase high performance liquid chromatography. One main fraction was collected and analyzed by mass spectrometry. One pentapeptide was identified from the main fraction of BSFOP-FE, and its amino acid sequence was Thr-Ser-Gly-Met-Pro. BSFOP-Fe could be applied as a food additive, to dietary nutrients, and to pharmaceutical products as an iron supplement.