摘要
研究采用DEAE-Sepharose F.F离子交换层析和Sephadex G-100凝胶过滤层析对嗜酸乳杆菌发酵液中的亚油酸异构酶进行了分离纯化,酶回收率为6.39,纯化倍数为37.9倍。经研究确定酶最适pH为6.0,最适反应温度为30℃。在pH 6~8之间,亚油酸异构酶可保持较高活力,超出此范围,酶活力明显下降;该酶对高温敏感,50℃保温2 h,酶活力即变得很低;亚油酸异构酶受底物LA的抑制,酶反应最适LA浓度为1.5×10-5g/mL,过高LA则对酶产生抑制作用。
Linoleate isomerase was isolated and purified from the fermentation broth of Lactobacillus acidophilus by DEAE-Sepharose F.F.ion exchange chromatography and Sephadex G-100 gel permeation chromatography.Recovery rate of linoleate isomerase was 6.39,purification was 37.9-fold.The optimal pH was 6.0,optimal reaction temperature was 30 ℃.The activity of linoleate isomerase maintained high at pH 6~8,the activity decreased beyond this range;the enzyme was sensitive to high temperature,the activity was very low after incubation at 50 ℃ for 2 h;linoleate isomerase was inhibited by the substrate（LA）,the optimal concentration of LA for the enzyme was 1.5×10-5 g/mL,linoleate isomerase will be inhibited by higher concentration of LA.
出处
《中国调味品》
CAS
北大核心
2010年第3期43-47,共5页
China Condiment
关键词
亚油酸异构酶
离子交换层析
凝胶过滤
酶活力
linoleate isomerase
ion exchange chromatography
Sephadex chromatography
enzyme activity
