摘要
目的:初步摸索出一条适合工业化开发、高效的、可溶表达结核分枝杆菌MTB8.1蛋白的发酵工艺。方法:利用菌株pUC18/MTB8.1/DH10B为发酵株,通过对培养基组成和发酵参数进行系统研究,从而获得一全新的发酵工艺。结果:重组结核分枝杆菌MTB8.1蛋白通过本发酵工艺的表达,单位体积发酵液可溶性蛋白的产量大幅提高,每升发酵液纯化得到可溶性蛋白约30 mg左右。结论:初步摸索出一条较好的MTB8.1在大肠埃希菌系统中的可溶性表达的途径,为其工业化生产奠定了理论基础。
Objective: To explore an effective fermentation process of Mycobacterium tuberculosis protein MTB8.1 with soluble expression, which would be suitable for industrial development. Methods: Strain pUC18/MTB8.1/DH10 B was used as fermentation strain and a systematic study of the composition of medium and the parameters of fermentation was conducted to obtain a new fermentation process. Results: By means of the new fermentation process, the yield of soluble recombinant protein MTB8.1 was greatly increased in per unit volume of fermentation broth, with about 30 mg of soluble protein obtained from every liter of fermentation broth through purification. Conclusion: A better way of soluble expression of MTB8.1 in Escherichia coli expression system was found tentatively, which laid the theoretical foundation for the industrial production.
出处
《大理学院学报(综合版)》
CAS
2014年第8期18-22,共5页
Journal of Dali University
基金
国家自然科学基金资助项目(81260456)
关键词
结核分枝杆菌
MTB8
1蛋白
可溶性表达
发酵工艺
抗原性
Mycobacterium tuberculosis
protein MTB8.1
soluble expression
fermentation process
antigenicity