牛乳中β-乳球蛋白的仿生亲和纯化  

Biomimetic affinity purification of β-lactoglobulin from bovine milk

作　　者：霍晨晰[1] 董德贤[1] 李荣秀[1] 

机构地区：[1]上海交通大学生命科学技术学院,上海200240

出　　处：《中国生化药物杂志》2010年第3期150-154,共5页Chinese Journal of Biochemical Pharmaceutics

基　　金：863项目(2007AA100506)

摘　　要：目的研究牛乳中β-乳球蛋白的仿生亲和分离技术。方法从仿生亲和介质库中筛选亲和配体,并进行吸附条件优化。结果得到可以特异吸附乳球蛋白的固定化三乙烯四胺亲和配体,确定最佳结合缓冲液为10mmol/L磷酸盐缓冲液(含0.15 mmol/L NaCl,pH7.0),在此条件下,可实现一步从牛乳中纯化乳球蛋白,其纯度达到95%以上,回收率为83.35%。测定得到固定化三乙烯四胺的最大吸附容量为52.54 mg/g干介质。结论固定化三乙烯四胺亲和介质可从牛乳中纯化出高纯度β-乳球蛋白,且纯化流程简便,介质吸附量较大(52.54 mg/g干介质),适合工业化生产。Purpose The method was established to isolate β-1actoglobulin（β-1g） from bovine milk. Methods A library of biomimetic affinity ligands was screened for 13-1g binding specificity and capacity. Affinity chromatography was carried out based on the synthetic ligand selected. Results Immobilized triethylene tetramine was found to be an affinity ligand specific for bovine β-1g and the optimal affinity buffer condition was PBS buffer（10 mmol/L, 0.15 mmol/L NaC1, pH 7.0）. By this ligand β-1g was one-step purified from bovine milk with a purity of more than 95% and recovery of 73.37%. The maximum adsorption quantity of this affinity matrix reaches 52.54 mg/g dry matrix. Conclusion Immobilized trieth- ylene tetramine can be used to purify β-1g from bovine milk, and it has great potential to be applied to large-scale purification of β-1g due to the simple operation and high treatment capacity.

关 键 词：Β-乳球蛋白 仿生亲和纯化 最大吸附量 

分 类 号：Q51[生物学—生物化学] TQ464.7[化学工程—制药化工]