摘要
依次采用碱性蛋白酶、木瓜蛋白酶和风味蛋白酶对猪股骨头胶原蛋白进行酶解,制备降血压肽。为了得到高活性、高纯度的降血压肽,依次采用超滤、离子交换层析、凝胶层析对酶解液进行分离纯化,采用体外检测方法测定各分离产物对血管紧张素转化酶活性的半抑制浓度(IC50值)。结果显示:猪骨酶解液经超滤分离获得分子质量小于5 ku的组分对血管紧张素转化酶的抑制活性最高,IC50值为1.400 2 mg/mL;该组分进行离子交换层析分离得4个组分,其中组分2的活性最高,IC50值为0.488 4 mg/mL;再将组分2进行凝胶层析分离得4个组分,其中组分2-2的活性最高,IC50值为0.195 3 mg/mL。
Anti-hypertensive peptides were prepared from pig femoral bones by sequential hydrolysis using alkaline protease, papain and flavourzyme. In order to obtain high activity and purity of anti-hypertensive peptides, ultrafiltration, ion exchange chromatography and gel permeation chromatography were used to separate the hydrolysates. The angioensin- I converting enzyme （ACE） inhibitory activity （IC50） of the separated fractions was determined in vitro. The results showed that the ultrafiltration fraction with molecular weight of less than 5 ku showed the highest ACE inhibitory activity, with an ICs0 value of 1.400 2 mg/mL. The fraction was then purified by ion exchange chromatography to obtain 4 peaks, among which peak 2 had the strongest ACE inhibitory activity with an IC50 value of 0.488 4 mg/mL. The peak 2 was further fractionated by gel permeation chromatography to obtain 4 sub-peaks, and the sub-peak 2-2 had the highest ACE-inhibitory activity with an IC50value of 0.195 3 mg/mL.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2014年第6期50-54,共5页
Food Science
关键词
酶解
降血压肽
超滤
离子交换层析
凝胶层析
血管紧张素转化酶半抑制浓度
enzymatic hydrolysis
anti-hypertensive peptides
ultrafiltration
ion exchange chromatography
gel permeationchromatography
half inhibitory concentration of angioensin- I converting enzyme
