摘要
利用凝胶过滤层析法从牛乳乳清分离蛋白中分离纯化β-乳球蛋白,然后利用美拉德反应制备β-乳球蛋白与低聚异麦芽糖结合产物。通过竞争和非竞争ELISA法检测该结合产物的抗原性,结果显示糖基化后的β-乳球蛋白的抗原性得到显著降低。利用双缩脲法和苯酚硫酸法测定该结合物的组成,结果显示该结合物中β-乳球蛋白和低聚异麦芽糖摩尔比为1:8。进而对该结合物进行凝胶过滤层析和SDS-聚丙烯酰胺凝胶电泳分析,结果显示该结合物相对分子量为44kDa,仍保持原有二聚体结构。
Bovine β-lactoglobulin was purified from whey protein isolate by gel filtration chromatography, β-lactoglobulin（β-LG）- isomaltooligosaccharide （IMO） conjugate was prepared by using the Maillard reaction then.ELISA assay of competitive and noncompetitive both indicated the antigenicity of β-LG-IMO conjugate was significantly reduced.The composition of the conjugate determined according to the biuret and phenol-sulfuric acid methods showed that the molar ratio of β-LG to IMO in the conjugate was 1 ：8 ,The results of gel filtration chromatography and SDS-PAGE assay indicated that the molecular weight was 44kDa, and still maintained in dimmer form.
出处
《食品工业科技》
CAS
CSCD
北大核心
2009年第7期85-87,90,共4页
Science and Technology of Food Industry
基金
"十一五"国家科技支撑计划子课题(2006BAD04A06)
教育部留学回国人员科研启动基金
关键词
Β-乳球蛋白
低聚异麦芽糖
糖基化
抗原性
β-lactoglobulin
isomaltooligosaccharide
saccharification
antigenicity
