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植物乳杆菌亚油酸异构酶的分离纯化及其性质研究
引用本文:苗士达,张中义,刘萍,柴秋儿,胡锦荣,孙君社. 植物乳杆菌亚油酸异构酶的分离纯化及其性质研究[J]. 食品与发酵工业, 2005, 31(3): 12-15
作者姓名:苗士达  张中义  刘萍  柴秋儿  胡锦荣  孙君社
作者单位:1. 中国农业大学食品科学与营养工程学院,北京,100083
2. 郑州轻工业学院食品科学与生物工程系,郑州,450002
基金项目:国家自然科学基金 (No .2 0 3760 84)
摘    要:经硫酸铵分级沉淀、阴离子交换层析和凝胶过滤,由植物乳杆菌(LactobacillusplantarumL 2 9)分离纯化得到亚油酸异构酶,分子量为4 3ku。对其酶学性质进行研究,结果表明,温度37℃、pH 6 0时酶活性较高;Co2 + 、Fe2 + 可提高酶的活性,Cu2 + 、Zn2 + 则对酶活力有抑制作用;该酶作用于亚油酸的Km=2 5 3×10 -5mol/L ,Vmax=2 5 7×10 -8mol/ (min·mg)。

关 键 词:植物乳杆菌  亚油酸异构酶  共轭亚油酸
修稿时间:2004-10-11

Purification and Characterization of a Linoleic Acid Isomerase from a Lactobacillus plantarum Bateria
Miao Shida,Zhang Zhongy,Liu Ping,Chai Qiuer,Hu Jinrong,Sun Junshe. Purification and Characterization of a Linoleic Acid Isomerase from a Lactobacillus plantarum Bateria[J]. Food and Fermentation Industries, 2005, 31(3): 12-15
Authors:Miao Shida  Zhang Zhongy  Liu Ping  Chai Qiuer  Hu Jinrong  Sun Junshe
Affiliation:Miao Shida 1 Zhang Zhongy 1,2 Liu Ping 1 Chai Qiuer 1 Hu Jinrong 1 Sun Junshe 1 1
Abstract:A linoleic acid isomerase was purified from Lactobacillus plantarum L-29 by ammonium sulfate precipitation,DEAE Sepharose fast flow and Sephadex G-100 column chromatography. The molecular weight of the enzyme was about 43ku. The enzyme exhibited higher activity when temperature and pH were 30℃,6.0 respectively. Co 2+ ,Fe 2+ improved the activity of the enzyme, and Cu 2+ ,Zn 2+ instead decreased the activity of the enzyme. Mcihael constants of the enzyme were K m=2.53×10 -5 ?mol/L and V max =2.57×10 -8 ?mol/(min·mg) when substrate was linoleic acid.
Keywords:Lactobacillus plantarum   linoleic acid isomerase   conjugated linoleic acid
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