摘要
本研究以燕麦蛋白为原料,分别选用Alcalase、Neutrase和Protamex进行单独或联合水解,经活性炭YD-303脱色、大孔吸附树脂DA-201CⅡ脱盐及分级纯化、SephadexG-25凝胶色谱柱进一步分离,以获得高纯度、高活性的血管紧张素转化酶(angiotensin converting enzyme,ACE)抑制肽。结果表明:单酶反应时,Alcalase水解2h所获得的产物对ACE的抑制率可达85.40%;YD-303处理燕麦蛋白酶解液脱色最优工艺为添加量1.5%(W/V)、pH3.5、温度40℃、脱色时间75min。利用75%乙醇洗脱大孔吸附树脂DA-201CⅡ所获得的组分ACE抑制活性最高,其经SephadexG-25进一步分离纯化,得到四个分离组分,第四组分的ACE抑制活性最高,抑制率为95.6%。
Oat protein was hydrolyzed by Alcalase, Neutrase, and Protamex individually or jointly and the obtained hydrolysates were further subjected to decolorization with activated carbon YD-303 and purification with macroporous adsorption resin DA201-C II for desalination and Sephadex G-25 column for fractionation. The results showed that the hydrolysates of oat protein by individual Alcalase had the highest ACE inhibitory activity of 85.40%. The optimum decolorization conditions with YD-303 contained quantity of activated carbon 1.5%, pH 3.5, 40℃, and adsorption time 75 min. Fractions eluted with 75% ethanol from macroporous adsorption resin displayed the highest inhibitory activity and were further separated by Sephadex G-25 into 4 subfractions. The fourth subfraction presented the most effective elution and its inhibitory activity was 95.6%.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2009年第11期189-193,共5页
Food Science
关键词
燕麦蛋白
酶解
ACE抑制肽
脱色
脱盐
oats protein
enzymatic hydrolysis
ACE inhibitory peptide
decolorization
desalination
