节点文献

鹰嘴豆蛋白Alcalase水解工艺及其体外抗氧化活性的研究

Enzymic hydrolysis of chickpea protein by Alcalase and its antioxidative activities

  • 推荐 CAJ下载
  • PDF下载
  • 不支持迅雷等下载工具,请取消加速工具后下载。

【作者】 李艳红; 江波; 刘柱; 张涛; 沐万孟;

【Author】 LI Yan-hong,JIANG Bo,LIU Zhu,ZHANG Tao,MU Wan-meng (Key Lab of Food Science and Safety,Ministry of Education,School of Food Science and Technology,Southern Yangtze University,Wuxi,Jiangsu 214036,China)

【机构】 江南大学食品学院食品科学与安全国家教育部重点实验室; 江南大学食品学院食品科学与安全国家教育部重点实验室 江苏无锡214036; 江苏无锡214036;

【摘要】 研究Alcalase蛋白酶水解鹰嘴豆蛋白的工艺、不同水解度鹰嘴豆蛋白水解产物的体外抗氧化能力以及分子量分布.在单因素基础上以水解度和还原能力为指标设计正交试验得到水解最佳条件为:温度50℃,[E]/[S]2%,pH值8.0,反应时间40 min.以此水解条件进行试验测得水解度为15.04%,还原能力为0.270;水解度(DH)为15%时鹰嘴豆蛋白水解产物的还原能力、清除DPPH自由基、清除羟基自由基(·OH)和抑制超氧阴离子能力最高.从分子排阻色谱图中可以看到,随着水解度的提高,肽的分子量分布总体表现为大分子量肽逐渐减少,小分子量肽的含量逐渐增加.而具有最佳体外抗氧化活性的鹰嘴豆蛋白水解产物的分子量主要集中在300~1500 Da之间.

【Abstract】 The optimal conditions for enzymatic hydrolysis of chickpea protein,the antioxidative activity,free radical scavenging activities and molecular weight distribution of the chickpea protein hydrolysates were studied.On the basis of single factor test,the optimal conditions of Alcalase were determined by orthogonal experiments from degree of hydrolysis(DH) and reducing power as follows: Temperature,50℃;[E]/ 2%;pH8.0;reaction time,40 min.Under this condition,DH was 15.04%,and the reducing power reached 0.270.Chickpea protein hydrolysate at DH 15 had the most powerful antioxidative activities and radical scavenging activites,such as reducing power,hydroxyl radical scavenging activity,scavenging of superoxide anion,DPPH radical scavenging activity.The molecular weight distribution profile of chickpea protein hydralysates at various DH exhibited that with the increase of DH,the molecular weight decreased accordingly and the ratio of peptide with molecular weight(Mw) between 300 to 1500 Da was highest in hydrolysate at DH15.

【基金】 国家自然科学基金资助项目(20436020)
  • 【文献出处】 浙江大学学报(农业与生命科学版) ,Journal of Zhejiang University(Agriculture and Life Sciences) , 编辑部邮箱 ,2007年04期
  • 【分类号】TS201.21
  • 【被引频次】42
  • 【下载频次】526
节点文献中: 

本文链接的文献网络图示:

本文的引文网络