嗜酸乳杆菌突变株产共轭亚油酸异构酶的纯化研究  

Purification of Conjugated Linoleic Acid Isomerase from Lactobacillus acidophilus Mutants

作　　者：孙晓琦[1] 廖玲[1] 吴风亮[2] 高莉莉[1] 赵宏飞[1] 裴家伟[2] 吕兆林[1] 张柏林[1] 

机构地区：[1]北京林业大学生物学院食品系,北京100083 [2]河北农业大学食品学院,河北保定071001

出　　处：《乳业科学与技术》2009年第6期254-258,共5页JOURNAL OF DAIRY SCIENCE AND TECHNOLOGY

基　　金：国家高技术研究发展计划(863计划)"高活性乳酸菌发酵剂制造关键技术(2006AA10Z344)"及"益生菌定向筛选与功能开发关键技术(2008AA10Z335)"资助项目

摘　　要：以嗜酸乳杆菌NCFM和Lakcid作为出发菌株,通过紫外诱变及化学诱变筛选得到突变株。代谢亚油酸生成共轭亚油酸(CLA),研究转化过程中的关键性酶-亚油酸异构酶的酶学性质,采用硫酸铵沉淀、透析等对该酶进行纯化,用SDS-PAGE测得该酶的亚基分子量为60.5 ku;并得出该酶的最适温度是44℃,最适pH是6.0左右,金属离子Fe2+、K+等对异构酶的反应有促进作用,Zn2+等对反应都起抑制作用。Two mutants out of Lactobacillus aeidophilus strains NCFM and Lakcid, obtained by ultraviolet and chemomorphosistheir, could catalyze linoleie acid into conjugated linoleic acid （CLA） due to the existence of isomerase in 2 mutant＇s cells. The conjugated linoleic acid isomerase, purified by （NH4）2SO4 fraetionation, dialysis and Sephadex G-100 gel filtration chromatography, had relative molecular weight of 60.5 ku with the enzyme subunit by SDS-PAGE. The enzyme had an optimum reaction temperature of 44℃ and pH 6.0, respectively. The activity of enzyme could be activated by Fe^2＋,K^＋, while inhibited by Zn^2＋.

关 键 词：嗜酸乳杆菌 突变株 亚油酸异构酶 纯化 

分 类 号：Q814.1[生物学—生物工程]