食品科学2011，Vol.32Issue(17)：262-268,7.
发酵乳杆菌细胞壁蛋白酶的分离纯化及酶学性质研究
Purification and Enzymatic Properties of Cell Envelope Protease from Lactobacillus fermentum
摘要
Abstract
The purification process of cell envelope protease（CEP） from Lactobacillus fermentum was explored in this paper.Cells were suspended in 50 mmol/L Tris-HCl（pH 7.8） and subjected to ultrasonication（cell concentration of 0.06 g/mL,ultrasonic power of 330 W,ultrasonic treatment time of 3 s with intermission of 5 s,and repeated ultrasonic treatment number of 220）.The supernatant was collected,precipitated with 60% saturated（NH4）2SO4 solution and separated by Sephacryl S-300 HR chromatography.The active protease was recovered from Native-PAGE gel.The ACE inhibitory rate of purified CEP was 50%.The molecular mass of purified CEP estimated by SDS-PAGE was approximately 32.5 kD.Maximum activity was reached at pH 8.0 and 41℃.The activity of CEP could be activated by Mg2＋,Co2＋ and Ca2＋ and inhibited by Zn2＋,Ni2＋ and PMSF,suggesting that CEP belongs to serine protease.On the other hand,its activity could also be inhibited by EDTA,suggesting that CEP is a metallopeptidase.关键词
发酵乳杆菌/细胞壁蛋白酶/纯化/酶学性质Key words
Lactobacillus fermentum/cell envelope protease/purification/enzymatic properties分类
轻工纺织引用本文复制引用
朱姁,潘道东..发酵乳杆菌细胞壁蛋白酶的分离纯化及酶学性质研究[J].食品科学,2011,32(17):262-268,7.基金项目
国家自然科学基金项目 （）
江苏省科技支撑计划项目 （）
浙江省重大科技专项 （）
