论文部分内容阅读
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。
Followed by alkaline protease, papain and flavor protease porcine femoral head collagen protein hydrolysis, preparation of antihypertensive peptides. In order to obtain high activity, high-purity antihypertensive peptides, followed by ultrafiltration, ion exchange chromatography, gel chromatography on the separation and purification of the hydrolyzate, in vitro detection of each isolated product of angiotensin converting enzyme activity Semi-inhibitory concentration (IC50 value). The results showed that the components with molecular weight of less than 5 ku obtained by ultrafiltration were the highest inhibitory activity against angiotensin converting enzyme with the IC50 of 1.400 2 mg / mL. The constituents were separated by ion exchange chromatography There were four components, of which component 2 had the highest activity with an IC50 value of 0.488 4 mg / mL. Then component 2 was separated by gel filtration and four components were obtained, of which component 2-2 had the highest activity, The IC50 value is 0.195 3 mg / mL.