摘要
通过利用原子力显微镜(AFM)来观察凝胶过滤层析法提纯短乳杆菌M8菌株的S-层蛋白的表面形貌,同时探讨S-层蛋白的再生特性及黏附特性。结果表明:凝胶过滤层析法能够获得纯度较高的S-层蛋白;该蛋白在纯水中可自我组装成纳米级"团簇"结构;去除S-层蛋白的菌体细胞仍然具有生命活性,适当培养后可重新表达该蛋白;短乳杆菌M8可黏附到Caco-2细胞上,其S-层蛋白介导此过程。
The aim of this study was to purify S-layer proteins from Lactobacillus brevis M8, isolated from fresh milk, by Sephadex G-75 column chromatography and observe their surface morphology under atomic force microscope (AFM). Also, regeneration and adhesion characteristics were explored. Highly pure S-layer proteins were obtained by Sephadex G-75 column chromatography, which could form nano-cluster by self-assemblage. Lactobacillus brevis M8 cells without S-layer proteins could re-express the proteins after re-incubation. Lactobacillus brevis M8 could adhere to Caco-2 cells, which was mediated by the S-layer proteins.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2012年第7期172-175,共4页
Food Science
基金
国家"863"计划项目(2007AA10Z347)
湖南省研究生科研创新项目(54040108005/12254)
关键词
短乳杆菌M8
S-层蛋白
AFM形貌
黏附
Lactobacillus brevis M8
S-layer proteins
atomic force microscope (AFM) images
adhesion