Dept of Food and Analytical Chemistry, University of Vigo, 32004 Ourense, Spain.
Biotechnol Prog. 2012 Sep-Oct;28(5):1197-206. doi: 10.1002/btpr.1587. Epub 2012 Jul 26.
Three mathematical models, two logistic models (previously published in previous works) and one mechanistic, developed in this work and based on Michaelis-Menten kinetics, were compared to select the most adequate model in describing the angiotensin-converting enzyme (ACE)-inhibitory activity of bioactive peptide mixtures obtained from cheese whey protein. The significance of both the model and its parameters as well as the value of the regression coefficient was used as criteria to select the most adequate model for obtaining the IC(50) values corresponding to each bioactive peptides mixture. The best results were obtained with the Michaelis-Menten-based model because it provided the best fits and in addition the values for its parameters were always significant. As parameters of this model have a physical meaning, it could be used for inhibition-testing experiments in the development of novel bioactive peptides. The results obtained indicated that the peptide mixture derived from the neutrase hydrolysis exhibited strong ACE inhibition activity. The main active peptides were short, with molecular masses below 1 kDa (IC(50) = 40.37 ± 2.66 μg/mL) and represent 38% of the initial protein content in the hydrolysate.
三种数学模型，两种逻辑斯蒂模型（先前在以前的工作中发表过）和一种基于米氏动力学的机械模型，在这项工作中被开发出来，并被用来比较选择最适合描述从奶酪乳清蛋白获得的生物活性肽混合物的血管紧张素转化酶（ACE）抑制活性的模型。模型及其参数的显著性以及回归系数的值被用作选择最适合获得对应于每种生物活性肽混合物的 IC（50）值的模型的标准。基于米氏动力学的模型提供了最佳的拟合效果，并且其参数的值总是显著的，因此获得了最好的结果。由于该模型的参数具有物理意义，因此它可以用于新型生物活性肽的抑制测试实验中。得到的结果表明，来自中性蛋白酶水解的肽混合物表现出强烈的 ACE 抑制活性。主要的活性肽短，分子量低于 1 kDa（IC（50）= 40.37 ± 2.66 μg/mL），占水解物初始蛋白质含量的 38％。
