Department of Food Science and Engineering, College of Biological Sciences and Technology, Beijing Key Laboratory of Forest Food Process and Safety, Beijing Forestry University , Beijing 100083, China.
Food Science and Engineering College, Beijing University of Agriculture , Beijing 102206, China.
J Agric Food Chem. 2015 Nov 4;63(43):9543-9. doi: 10.1021/acs.jafc.5b04016. Epub 2015 Oct 22.
Peptides released from oat, buckwheat, and highland barley proteins were examined for their in vitro inhibitory effects on dipeptidyl peptidase IV (DPP4), an enzyme that deactivates incretin hormones involved in insulin secretion. All of the hydrolysates exhibited DPP4 inhibitory activities, with IC50 values ranging from 0.13 mg/mL (oat glutelin alcalase digestion) to 8.15 mg/mL (highland barley albumin tryptic digestion). The lowest IC50 values in gastrointestinal, alcalase, and tryptic digestions were 0.99 mg/mL (oat flour), 0.13 mg/mL (oat glutelin), and 1.83 mg/mL (highland barley glutelin). In all, 35 peptides of more than seven residues were identified in the tryptic hydrolysates of oat globulin using liquid chromatography-mass spectroscopy. Peptides LQAFEPLR and EFLLAGNNK were synthesized and their DPP4 inhibitory activities determined. LQAFEPLR showed high in vitro DPP4 inhibitory activity with an IC50 value of 103.5 μM.
从燕麦、荞麦和青稞蛋白中释放的肽被检测其对二肽基肽酶 IV(DPP4)的体外抑制作用,DPP4 是一种使参与胰岛素分泌的肠降血糖素失活的酶。所有水解产物均表现出 DPP4 抑制活性,IC50 值范围从 0.13 mg/mL(燕麦谷蛋白碱性蛋白酶消化)到 8.15 mg/mL(青稞白蛋白胰蛋白酶消化)。在胃肠道、碱性蛋白酶和胰蛋白酶消化中,IC50 值最低的分别为 0.99 mg/mL(燕麦粉)、0.13 mg/mL(燕麦谷蛋白)和 1.83 mg/mL(青稞谷蛋白)。使用液相色谱-质谱法在燕麦球蛋白的胰蛋白酶水解物中鉴定出 35 种超过七个残基的肽。合成了肽 LQAFEPLR 和 EFLLAGNNK,并测定了它们的 DPP4 抑制活性。肽 LQAFEPLR 表现出高体外 DPP4 抑制活性,IC50 值为 103.5 μM。