基于二次通用旋转设计的蓝蛤ACE抑制肽酶解工艺模型

以蓝蛤蛋白为原料,选用Protamex蛋白酶进行酶解并以水解度作为测定指标,在单因素实验基础上进行二次通用旋转设计,对获得最优工艺参数进行验证,将获得的血管紧张素转化酶(ACE)抑制肽进行ACE抑制活性测定和傅立叶红外光谱分析。结果表明在底物浓度为10%,酶解p H为10,加酶量7%和酶解温度60℃为最优酶解条件,酶解1 h所得的蓝蛤蛋白水解度为30.1%,利用高效液相色谱法对蓝蛤活性肽进行体外ACE抑制活性测定表明其半抑制浓度为80 mg/m L,且活性肽溶液以无规卷曲空间构型为主。 

Enzyme hydrolysis preparation model of ACE inhibitory peptides from blue clam based on quadratic general rotation design

Blue clam was hydrolyzed by protamex protease and measured by the degree of hydrolysis. The hydrolysis model of peptides from blue clam was established through quadratic general rotation design followed single factor experiment,subsequently ACE inhibitory activity and FTIR of blue clam-derived peptides was measured. The results showed that the equation for the optimal regression equation had a maximal value according to regression coefficient test,regression equation,and the lack of fit test. The optimal details of enzymatic hydrolysis was as follows:substrate concentration 10%,enzymatic hydrolysis p H value 10,the amount of enzyme 7% and hydrolysis temperature 60 ℃,and hydrolysis degree of blue clam protein was 30.1% in one hour. In vitro ACE inhibitory activity of bioactive peptides from blue clam was performed by high performance liquid chromatography,and the IC_(50) value was 80 mg/m L. In addition,secondary structure of the blue calm-derived peptides was random coil.