| 乌鸡低聚肽亚铁螯合物的分离纯化与结构鉴定 |
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| 引用本文： | 刘文颖,鲁军,宋莎莎,谷瑞增,任迪峰,蔡木易.乌鸡低聚肽亚铁螯合物的分离纯化与结构鉴定[J].现代食品科技,2017,33(8):95-102. |
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| 作者姓名： | 刘文颖 鲁军 宋莎莎 谷瑞增 任迪峰 蔡木易 |
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| 作者单位： | （1.中国食品发酵工业研究院，北京市蛋白功能肽工程技术研究中心，北京 100015）,（1.中国食品发酵工业研究院，北京市蛋白功能肽工程技术研究中心，北京 100015）,（2.北京林业大学生物科学与技术学院，北京 100083）,（1.中国食品发酵工业研究院，北京市蛋白功能肽工程技术研究中心，北京 100015）,（2.北京林业大学生物科学与技术学院，北京 100083）,（1.中国食品发酵工业研究院，北京市蛋白功能肽工程技术研究中心，北京 100015） |
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| 基金项目： | 国家十三五重点研发计划（2016YFD0400604）；国家高技术研究发展计划（863计划）项目（2013AA102205-02） |
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| 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。
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| 关 键 词： | 乌鸡 特性 低聚肽 肽铁螯合物 结构鉴定 |
| 收稿时间： | 2017/1/18 0:00:00 |
Isolation and Structural Identification of Iron (II)-Chelated Oligopeptides from Black-Bone Silky Fowl |
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| LIU Wen-ying,LU Jun,SONG Sha-sh,GU Rui-zeng,REN Di-feng and CAI Mu-yi.Isolation and Structural Identification of Iron (II)-Chelated Oligopeptides from Black-Bone Silky Fowl[J].Modern Food Science & Technology,2017,33(8):95-102. |
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| Authors: | LIU Wen-ying LU Jun SONG Sha-sh GU Rui-zeng REN Di-feng and CAI Mu-yi |
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| Affiliation: | (1.Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, China),(1.Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, China),(2.College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China),(1.Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, China),(2.College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China) and (1.Beijing Engineering Research Center of Protein and Functional Peptides, China National Research Institute of Food and Fermentation Industries, Beijing 100015, China) |
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| 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. |
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| Keywords: | black-bone silky fowl characteristic low-molecular-weight peptides iron-chelated peptides structure identification |
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