食品科学 ›› 2007, Vol. 28 ›› Issue (12): 305-308.

• 生物工程 • 上一篇    下一篇

嗜酸乳杆菌亚油酸异构酶的分离纯化研究

 王武, 付敏, 唐晓明, 潘见   

  1. 合肥工业大学生物与食品工程学院; 农产品生物化工教育部工程研究中心 安徽合肥230009农产品生物化工教育部工程研究中心; 安徽合肥230009;
  • 出版日期:2007-12-15 发布日期:2011-11-22

Study on Purification of Lionleic Ismerase from Lactobacillus acidophilus

 WANG  Wu, FU  Min, TANG  Xiao-Ming, PAN  Jian   

  1. 1.School of Biotechnology and Food Engineering, Hefei University of Technology, Hefei 230009, China; 2.Engineering Research Center of Bio-process, Ministry of Education, Hefei 230009, China
  • Online:2007-12-15 Published:2011-11-22

摘要: 本实验对嗜酸乳杆菌亚油酸异构酶的分离纯化进行了研究。嗜酸乳杆菌的粗酶液经40%~80%饱和度的硫酸铵盐析、透析、SephadexG-100凝胶过滤层析等步骤进行分离纯化后,酶的纯化倍数达到3.10,比活力为475.75U/(mg蛋白质);纯化后的亚油酸异构酶在SDS-PAGE电泳中只呈现一条带,并测得分子量约为46.6kDa。

关键词: 嗜酸乳杆菌, 亚油酸异构酶, 分离纯化, SDS-PAGE电泳

Abstract: The purification of Lionleic ismerase in Lactobacillus acidophilus were studied in this paper. Crude enzyme from Lactobacillus acidophilus was purified by ammonium sulfate solution of 40%~80%, dialysis and Sephadex G-100 gel fractionation chromatography, achieving an overall purification of 3.10-fold and a spectic activity of 475.45[U/(mg protein)]. The purified enzyme was a single distinct protein band by SDS-PAGE, with an estimated molecular weight of about 46.6 kDa.

Key words: Lactobacillus acidophilus, lionleic ismerase, purification, SDS-PAGE