School of Food Science and Technology, National Engineering Research Center of Seafood, Dalian Polytechnic University, Dalian 116034, China; Department of Food Science and Engineering, School of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin 150001, China.
College of Food Science, Northeast Agricultural University, Harbin 150030, China.
Food Chem. 2018 Aug 1;256:98-104. doi: 10.1016/j.foodchem.2018.02.107. Epub 2018 Feb 21.
Various bioactive peptides are continuously being identified from casein hydrolysates. In this work, a novel angiotensin I-converting enzyme (ACE)-inhibitory (ACEI) peptide, NMAINPSKENLCSTFCK, derived from the α-casein fragment residues 25-41, was screened and identified by UPLC-ESI-Q-TOF-MS/MS from tryptic casein hydrolysate. The IC value of the peptide, determined by an HPLC method, was 129.07 μM. The Lineweaver-Burk plot showed that this peptide acted as a mixed-type inhibitor against ACE, which might be attributed to the peptide being susceptible to degradation by ACE, indicating that the mixed-type inhibition could partly be a result of newly generated peptide fragments. The physicochemical characteristics and the secondary structure were evaluated by circular dichroism analysis and online prediction software (Expasy, PepDraw, and ProtParam) to identify the basic characteristics of this peptide. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACEI activity of the peptides.
各种生物活性肽不断从酪蛋白水解物中被鉴定出来。在这项工作中,一种新型的血管紧张素转换酶(ACE)抑制肽,NMAINPSKENLCSTFCK,是从小牛酪蛋白片段 25-41 衍生而来的,通过 UPLC-ESI-Q-TOF-MS/MS 从胰蛋白酶酪蛋白水解物中筛选和鉴定。肽的 IC 值通过 HPLC 方法测定为 129.07 μM。Lineweaver-Burk 图表明,该肽对 ACE 表现出混合抑制作用,这可能归因于肽易被 ACE 降解,表明混合抑制可能部分是由于新生成的肽片段所致。通过圆二色性分析和在线预测软件(Expasy、PepDraw 和 ProtParam)评估该肽的物理化学特性和二级结构,以确定该肽的基本特性。此外,通过 Discovery Studio 2017 R2 软件模拟分子对接,提供肽的 ACEI 活性的潜在机制。