摘要
大豆贮藏蛋白主要包括大豆球蛋白(Glycinin)和伴大豆球蛋白(Conglycinin),本研究采用Sephadex-G15凝胶过滤和薄层层析的方法,对伴大豆球蛋白胃蛋白酶水解产物中促双歧杆菌增殖肽进行分离,所得活性组分通过毛细管HPLC及质谱进行鉴定,结果表明,分离得到促双歧杆菌增殖活性最强的组分是由性质相近的肽混合物组成,通过毛细管HPLC可以得到活性酶解肽的图谱,并通过质谱可知酶解肽主要由6-10个氨基酸残基组成。上述结果提示,伴大豆球蛋白中的生物活性物质是以无活性的形式存在于蛋白质的多肽链中,必须通过适当酶解,在一定条件下才能释放出来,发挥出各种生物学功能。
Soybean storage proteins are composed mainly of two major components, conglycinin and glyoinin. The purpose of the present study was to investigate which peptides, capable of enhancing the growth of bifidobacteria, are liberated from conglycinin during pepsin hydrolysis. Components of pepsin -treated conglycinin were separated using Sephadex -G15 gel filtration chromatography and TLC, the resulting fractions were analyzed for enhancing bifidobacteria activity. Further purification was conducted with Capillary HPLC guided by the active assay, and fragments were identified by means of Matrix -Assisted Laser Desorption lonization Time of Flight Mass Spectrometry (MALDI-TOF-MS).Using this strategy, our results showed that the most active fraction which stimutates the growth of bifidobacteria was the mixture of peptides, peptide mapping was got by Capillary HPLC, and the molecular mass was obtained with MALDI -TOF Mass Spectrometry. The results indicated that the bifidobacteria -stimulating activity was found in hydrolysate, but not in original conglycinin.
出处
《食品工业科技》
CAS
CSCD
北大核心
2005年第4期83-85,88,共4页
Science and Technology of Food Industry
基金
国家自然科学基金资助项目(30070565)
关键词
伴大豆球蛋白
水解肽
分离纯化
鉴定
双歧杆菌
conglycinin
hydrolysis-peptide
separation and purification
determination
bifidobacteria
