机构地区: 广西大学化学化工学院
出 处: 《中国乳品工业》 2012年第10期18-20,32,共4页
摘 要: 以水牛乳蛋白为原料,选用6种蛋白酶在各自适宜的条件下酶解制备血管紧张素转化酶(ACE)抑制肽,用高效液相色谱检测酶解产物对ACE的体外抑制活性,筛选出胃蛋白酶为制备水牛乳蛋白ACE抑制肽的最佳用酶。在此基础上,分别考察了酶解时间、初始酶用量、初始底物浓度、酶解温度和pH值对酶解工艺的影响,得到水牛乳蛋白制备ACE抑制肽的适宜酶解工艺条件:酶解时间为3 h,酶用量为10 000 U/g,底物质量浓度为20 g/L,反应温度为37℃,pH值为2.0,此时酶解产物的水解度为17.4%,ACE抑制率可达90.0%。采用超滤技术对酶解产物活性组份进行分离富集,结果表明产物中高活性部分均可富集于10 ku和5 ku渗透液中,且高活性组份分子量主要集中在5 ku以下,该组份对ACE的活性抑制率为84.7%。 The buffalo milk protein was hydrolyzed by six different proteolytic enzymes in their optional conditions to product angiotensin I converting enzyme (ACE) inhibitory peptides. The inhibition percent (IP) of ACE by the hydrolysates was detected with high performance liquid chromatography. The results showed the pepsin was the best enzyme for producing ACE inhibitory peptides. The hydrolysis time, en-zyme concentrations ([E]), substrate concentrations ([S]), hydrolysis temperatures and pH values were investigated. The optimal conditions for producing ACE inhibitory peptides were as follows: [E] in 10000 U/g, [S] in 20 g/L, hydrolysis temperature at 37 ℃, pH 2.0 and hydrolysis time in 3 h. Under this conditions the hydrolysis degree was 15.8 % and the IP was 90 %. Furtheromre, the hydrolysates was seperated by ul-trafiltration. The results showed that 10 ku permeate and 5 ku permeate had higher activity. It was also found that 5 ku permeate was with highest activity and the IP was 84.7 %.
领 域: [化学工程]