食品科学 ›› 2007, Vol. 28 ›› Issue (1): 155-158.

• 生物工程 • 上一篇    下一篇

嗜酸乳杆菌亚油酸异构酶活力测定的研究

 曹健, 王月囡, 王红军, 王育军, 于海东   

  1. 河南工业大学生物工程学院; 河南工业大学生物工程学院 河南郑州450052; 河南郑州450052;
  • 出版日期:2007-01-15 发布日期:2011-12-31

Research on Enzyme Activity Assay of Lactobacillus acidophilus Linoleate Isomerase

 CAO  Jian, WANG  Yue-Nan, WANG  Hong-Jun, WANG  Yu-Jun, YU  Hai-Dong   

  1. College of Biological Engineering, Henan University of Technology, Zhengzhou, Henan 450052, China
  • Online:2007-01-15 Published:2011-12-31

摘要: 亚油酸异构酶能催化亚油酸转化为具有生理活性的共轭亚油酸。有关该酶活力的测定方法在国内外不同的文献中差别较大,尚没有统一的方法。本文对嗜酸乳杆菌亚油酸异构酶活力的测定方法进行了研究,以期为该酶分离纯化过程中酶活力的测定提供参考。通过单因素试验和正交试验,确定了该酶的最佳酶反应条件为:粗酶液添加量0.10ml,亚油酸0.70ml,Tween-802.00ml,反应温度37℃,反应时间3h。

关键词: 嗜酸乳杆菌, 亚油酸异构酶, 酶活力测定

Abstract: Linoleate isomerase can catalyze the chemical reaction from linoleic acid to conjugated linoleic acid, while the latter shows many physiological activities. However, linoleate isomerase activity assay differs from literature to literature. Enzyme activity assay of linoleate isomerase of Lactobacillus acidophilus was studied in this paper, so as to provide some reference to study the enzyme activity during the process of enzyme purification. Optimum reaction conditions for linoleate isomerase activity were determined by single-factor test and orthogonal test, as follows: crude enzyme 0.10ml, linoleic acid 0.70ml, Tween-80 2.00ml, reaction temperature 37℃, and reaction time 3h.

Key words: Lactobacillus acidophilus, linoleate isomerase, enzyme activity mensuration