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蛋清肽的结构及活性研究

Characterization and activity of bioactive peptide derived from egg white protein

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【作者】 于志鹏赵文竹于一丁刘静波

【Author】 YU Zhi-peng,ZHAO Wen-zhu,YU Yi-ding,LIU Jing-bo~* (Laboratory of Nutrition and Functional Food,College of Quartermaster Technology, Jilin University,Changchun 130062,China)

【机构】 吉林大学军需科技学院营养与功能食品研究室

【摘要】 蛋清蛋白质活性肽经交联葡聚糖凝胶色谱纯化,通过液相色谱四极杆线性离子阱串联质谱确证3种活性肽的一级结构,氨基酸序列分别为Arg-Val-Pro-Ser-Leu-Met,Thr-Pro-Ser-Pro-Arg和Asp-Leu-Gln-Gly-Lys。Fmoc固相合成法合成相应肽序列,经制备液相色谱纯化纯度分别为98.73%、98.77%、96.68%。利用分析型高效液相色谱分别测定3种肽的血管紧张素转化酶抑制活性,结果表明Asp-Leu-Gln-Gly-Lys的活性较高,血管紧张素转化酶活性抑制率为35%。

【Abstract】 In the present work,bioactive peptides derived from egg white protein were purified by gel filtration,and identified by high performance liquid chromatography tandem mass spectrogram.3 peptides,Arg-Val-Pro-Ser-Leu-Met, Thr-Pro-Ser-Pro-Arg and Asp-Leu-Gln-Gly-Lys were characterized,and synthesisd by Fmoc solid-phase synthesis.Purification of Arg-Val-Pro-Ser-Leu-Met,Thr-Pro-Ser-Pro-Arg and Asp-Leu-Gln-Gly-Lys were 98. 73%,98.77%,96.68%,respectively.The peptide,Asp - Leu - Gln - Gly - Lys,has the high angiotensin converting enzyme inhibitory activity;the value of activity property was 35%.

  • 【会议录名称】 2009食品科技(北京)论坛会议指南
  • 【会议名称】2009食品科技(北京)论坛
  • 【会议时间】2009-12-07
  • 【会议地点】中国北京
  • 【分类号】Q51
  • 【主办单位】北京食品学会、北京食品协会、《食品工业科技》杂志社
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