食品科学 ›› 2008, Vol. 29 ›› Issue (7): 243-246 .

• 生物工程 • 上一篇    下一篇

嗜酸乳杆菌亚油酸异构酶的酶学性质研究

王武,唐晓明,付敏,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:2008-07-15 发布日期:2011-07-28

Study on Enzymological Properties of Linoleic Acid Isomerase from Lactobacillus acidophilus

 WANG  Wu, TANG  Xiao-Ming, FU  Min, 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:2008-07-15 Published:2011-07-28

摘要: 本实验对嗜酸乳杆菌亚油酸异构酶的酶学性质进行了研究。结果表明:以亚油酸为底物,亚油酸异构酶的最适反应温度为40℃;最适反应pH值为4.0,pH值在3.0~6.0范围内有较高的稳定性;不同的金属离子和有机试剂对亚油酸异构酶的影响程度不同,同一种金属离子和有机试剂在不同浓度下也不相同;以亚油酸为底物的酶促反应米氏常数Km=33.33mol/L,Vmax=15.6mol/L·h。

关键词: 嗜酸乳杆菌, 亚油酸异构酶, 酶学性质

Abstract: The lionleic acid ismerase from Lactobacillus acidophilus was extracted to study its enzymological properties. The results indicated that the optimum temperature and pH value of lionleic acid ismerase are 40 ℃ and 4 respectively, and the ismerase exhibits strong stability to temperture (20 ~50 ℃) and pH value (4.0~6.0) for 1 h. Various metal ions and their respective concentrations have various effects on activity of the ismerase, and organic solvent as well. The Km of the ismerase is 33.33 mmol/L, and the Vmax is 15.6 mmol/L·h.

Key words: Lactobacillus acidophilus, lionleic acid ismerase, enzymological properties