文档介绍：48 2007, Vol. 28, No. 07 食品科学※基础研究
强阳离子交换色谱法从牛初乳中
分离纯化乳铁蛋白的研究
卢蓉蓉 1,2,许时婴 2,王璋 2,杨瑞金 1,2
(,江苏无锡 214122;
,江苏无锡 214122)
摘要:本实验研究了离子交换色谱技术大规模纯化乳铁蛋白的色谱条件。选用的 SP Sepharose Fast Flow 离子交换
剂对乳铁蛋白有很好的吸附选择性,洗脱速度可达到 2L/h。以 pH 值为 ~,10mmol/L 的磷酸盐为起始缓冲
液,通过改变离子强度进行分步洗脱。先采用 的 NaCl 溶液选择性洗脱分泌型免疫球蛋白 A 和乳过氧化物
酶组分,再采用 1mol/L 的 NaCl 洗脱 LF 组分。经 SDS-PAGE 测定,所得乳铁蛋白组分显示为单一区带,相对分
子质量为 80400Da。经等点聚焦测定,所得乳铁蛋白的等电点为 。中试生产的精制品中乳铁蛋白的纯度和回
收率分别为 % 和 %。
关键词:乳铁蛋白;分离纯化;强阳离子交换色谱;中试规模
Purification of Lactoferrin from Bovine Colostrum with Strong Cation Exchange
Chromatography on Pilot Scale
LU Rong-rong1,2,XU Shi-ying2,WANG Zhang2,YANG Rui-jin1,2
( Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China;
of Food Science and Technology, Jiangnan University, Wuxi 214122, China)
Abstract :A stepwise procedure for purification of lactoferrin (LF) extracted from bovine colostrum by ion exchange
chromatography on a pilot scale was investigated. SP Sepharose Fast Flow (SP Sepharose FF) of excellent absorption speciality
for LF, was chosen as the ion exchanger with elution rate of 2 L/h. mol/L NaCl aqueous solution was used to elute the secretory
immunoglobulin A and lactoperoxidase. Then, lactoferrin was eluted with mol/L NaCl aqueous buffer. Lactoferrin fraction is