摘要
以糖基化大豆蛋白为原料,经碱性蛋白酶酶解制得具有抑制致病菌粘附功能的糖肽,并分析功能性糖肽的消化稳定性。酶解物用Sephadex G-25层析可获得表观分子量分别为20 000 Da、6 500 Da和小于3 000 Da组分。对酶解物胃蛋白酶和胰蛋白酶体外模拟依次消化2 h后,20 000~6 500 Da的大豆糖肽分子量变化不大,较稳定,而分子量小于3 000 Da的大豆糖肽中有5%被消化,稳定性略有变化。说明糖基化大豆蛋白酶解物其功能性成分可以较稳定存在于消化系统。
Using glyco-soyprotein as raw material,enzymolysed by alkaline protease to obtain glycopeptides with th function of inhibiting pathogenic bacteria adhesion,the digestion of glycopeptide stability was analyzed. Enzymolysed content with Sephadex G-25 chromatography could obtain molecular weight of 20 000 Da,6 500 Da and less than 3 000 Da components. After enzymolysed by Pepsin and trypsin in vitro 2 hours in sequence,glycopeptides molecular weight between 20 000 Da and 6 500 Da were relatively stable,but the molecular weight less than 3 000 Da had been digested 5%. It indicated that glycopeptides with functional ingredients could exist in the digestive system steadily.
出处
《大豆科学》
CAS
CSCD
北大核心
2015年第3期474-479,共6页
Soybean Science
基金
国家"十二五"科技支撑计划(2012BAD34B04)
关键词
糖基化
大豆蛋白
酶解物
消化
Glycosylation
Soyprotein
Hydrolysates
Digestion