Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera 9, 28049 Madrid, Spain.
Food Chem. 2013 Nov 15;141(2):1072-7. doi: 10.1016/j.foodchem.2013.03.056. Epub 2013 Mar 25.
Dipeptidyl peptidase-IV (DPP-IV) is a serine protease involved in the degradation and inactivation of incretin hormones that act by stimulating glucose-dependent insulin secretion after meal ingestion. DPP-IV inhibitors have emerged as new and promising oral agents for the treatment of type 2 diabetes. The purpose of this study was to investigate the potential of β-lactoglobulin as natural source of DPP-IV inhibitory peptides. A whey protein concentrate rich in β-lactoglobulin was hydrolysed with trypsin and fractionated using a chromatographic separation at semipreparative scale. Two of the six collected fractions showed notable DPP-IV inhibitory activity. These fractions were analysed by HPLC coupled to tandem mass spectrometry (HPLC-MS/MS) to identify peptides responsible for the observed activity. The most potent fragment (IPAVF) corresponded to β-lactoglobulin f(78-82) which IC50 value was 44.7μM. The results suggest that peptides derived from β-lactoglobulin would be beneficial ingredients of foods against type 2 diabetes.
二肽基肽酶-IV（DPP-IV）是一种丝氨酸蛋白酶，参与降解和失活肠促胰岛素激素，这些激素在餐后通过刺激葡萄糖依赖性胰岛素分泌起作用。DPP-IV 抑制剂已成为治疗 2 型糖尿病的新型有前途的口服药物。本研究旨在探讨β-乳球蛋白作为 DPP-IV 抑制肽的天然来源的潜力。富含β-乳球蛋白的乳清蛋白浓缩物用胰蛋白酶水解，并在半制备规模上通过色谱分离进行分级。收集的六个馏分中的两个显示出显著的 DPP-IV 抑制活性。这些馏分通过高效液相色谱-串联质谱（HPLC-MS/MS）进行分析，以鉴定负责观察到的活性的肽。最有效的片段（IPAVF）对应于β-乳球蛋白 f（78-82），其 IC50 值为 44.7μM。结果表明，源自β-乳球蛋白的肽将是针对 2 型糖尿病的食品的有益成分。
