玉米大豆ACE抑制肽及其功能性质研究

Functional Property and Inhibiting Activity towards ACE of Mixture of Corn Peptides and Soybean Peptides

为了综合利用植物蛋白资源,使其营养价值、生物活性提高,本文采用碱性蛋白酶对玉米大豆复配蛋白进行酶法改性,用试剂盒测定了酶解肽抑制血管紧张素Ⅰ转化酶(ACE)的活性,并比较了玉米蛋白和大豆蛋白复配物酶解前后溶解性、乳化性、起泡性等功能性质的变化,结果表明:在pH=8.0,温度55℃,[E]/[S]=0.5%,料液比1∶15,时间4h条件下酶解,其酶解肽的ACE抑制活性最高,抑制率达84.02%;与复配蛋白相比,复配肽的溶解性、乳化性、起泡性等功能性有较显著的改善,更有利于人体消化吸收和食品加工。

In order to improve the nutritional value and bioactivity of plant proteins and make better utilization, the complex of corn protein with soybean protein was hydrolyzed by Alcalase, and its activity of inhibiting angiotension I - converting enzyme （ACE） was determined by a ACE detection kit. The functional properties of the complex protein and the complex peptide were compared. Results show that the complex peptide exhibits the highest inhibiting ACE activity with inhibiting rate of 84.02% under the optimum enzymolysis conditions as pH 8.0, 55 ℃, [ E ]/[ S ] =0.5%, ratio of material and water 1： 15, and time 4h. Compared to the complex protein, the complex peptide exhibits better solubility, foaming ability, foam stability, and emulsifying ability, which would be in favor of human digestion and food processing.