食品科学 ›› 2009, Vol. 30 ›› Issue (15): 30-32.doi: 10.7506/spkx1002-6630-200915005

• 基础研究 • 上一篇    下一篇

鸡卵清蛋白多肽的纯化及抗氧化作用的研究

周国仪,成 静,陈栋梁* ,王阿敬,杨国燕,季金林   

  1. 中国多肽产业集团天天好生物制品有限公司科研中心
  • 收稿日期:2008-12-03 修回日期:2009-06-08 出版日期:2009-08-01 发布日期:2010-12-29
  • 通讯作者: 陈栋梁* E-mail:tallyho@public.wh.hb.cn

Purification and Antioxidant Activity of Peptides Derived from Egg White Proteins

ZHOU Guo-yi,CHENG Jing,CHEN Dong-liang*,WANG A-jing,YANG Guo-yan,JI Jin-lin   

  1. Application Research Centre for Peptide Substance, Wuhan Tallyho Biological Product Co. Ltd., China
    Polypeptide Group, Wuhan 430023, China
  • Received:2008-12-03 Revised:2009-06-08 Online:2009-08-01 Published:2010-12-29
  • Contact: CHEN Dong-liang*, E-mail:tallyho@public.wh.hb.cn

摘要:

采用Sephadex G-25、Sephadex G-15 葡聚糖凝胶柱层析法对鸡卵清蛋白多肽进行纯化。实验结果表明,鸡卵清蛋白多肽经Sephadex G-25 凝胶柱层析分离出7 个组分,其中组分3 抗氧化活性最高, 对DPPH 自由基的清除率达到63.80%。组分3 经Sephadex G-15 凝胶柱层析,蒸馏水洗脱,得到4 个组分,其中组分3-1 和3-2 具有较强的DPPH 自由基清除能力,清除率分别为84.02% 和81.17%。反相高效液相色谱图显示,组分3-1 主要有一种成分。

关键词: 鸡卵清蛋白多肽, 纯化, 抗氧化活性

Abstract:

The peptides derived from egg white proteins were fractionated on Sephadex G-25 gel filtration column and the fraction with the highest DPPH· radical scavenging activity was purified on Sephadex G-15 gel filtration column. A total of 7 fractions were obtained by Sephadex G-25 gel filtration chromatography and fraction 3 showed the highest antioxidant activity with a DPPH· radical scavenging rate of 63.80% at 3 mg/ml. Fraction 3 was further separated into 4 subfractions, among which, subfraction 3-1 and 3-2 showed higher DPPH radical scavenging activities and the DPPH radical scavenging rates at 3 mg/ml were 84.02% and 81.17%, respectively. According to RP-HPLC chromatogram subfraction 3-1 had a high homogeneous composition.

Key words: peptides derived from egg white proteins, purification, antioxidant activity

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