Department of Nutrition and Dietetics, Faculty of Health Sciences, University of Health Sciences, 34668 Istanbul, Turkey.
Department of Nutrition and Dietetics, Faculty of Health Sciences, University of Health Sciences, 34668 Istanbul, Turkey.
Food Res Int. 2018 Sep;111:574-581. doi: 10.1016/j.foodres.2018.05.068. Epub 2018 Jun 2.
Food-derived opioid peptides that are released from proteins by digestion, fermentation, or food production processes lead to several health problems. The opioids are generally resistant to hydrolyze by proteases, except the dipeptidyl peptidase IV (DPPIV, EC 3.4.14.5) enzyme, because of proline amino acid. β-casomorphin (BCM) from milk casein, gluteomorphin (GM) from wheat gluten, and soymorphin (SM) from the soybean β-conglycinin β-subunit are natural substrates of DPPIV because of their amino acid sequences and proline location. In the present study, DPPIV from Lactococcus lactis spp. lactis was purified and characterized by mass spectrometry. Purified DPPIV was added to standard BCM, GM, and SM, and hydrolysis percentages of morphins were measured by HPLC analysis. The results indicated that DPPIV enzyme hydrolyzed food-derived opioids (from 0.1 mM to 2 mM), BCM (33.42% for 2 mM), SM (83.81% for 2 mM), and GM (45.73% for 2 mM) in vitro. Hydrolysis percentages of SM were considerably higher than the same concentrations with BCM and GM. For dietary supplements to be promising for reducing the adverse effects of food derived opioids, this must be supported by in vivo studies of DPPIV use in the human body.
由蛋白质消化、发酵或食品生产过程中释放的食物来源的阿片肽会导致多种健康问题。这些阿片肽通常对蛋白酶具有抗性，不易水解，除了二肽基肽酶 IV（DPPIV，EC 3.4.14.5）酶，因为其中含有脯氨酸氨基酸。牛奶酪蛋白中的β-酪啡肽（BCM）、小麦面筋中的谷氨酰吗啡（GM）和大豆β-伴球蛋白β-亚基中的大豆吗啡（SM）由于其氨基酸序列和脯氨酸位置，是 DPPIV 的天然底物。在本研究中，通过质谱法对乳球菌乳亚种的 DPPIV 进行了纯化和表征。将纯化的 DPPIV 加入到标准的 BCM、GM 和 SM 中，并通过 HPLC 分析测量吗啡的水解百分比。结果表明，DPPIV 酶在体外可水解食物来源的阿片肽（从 0.1mM 到 2mM）、BCM（2mM 时为 33.42%）、SM（2mM 时为 83.81%）和 GM（2mM 时为 45.73%）。SM 的水解百分比明显高于相同浓度的 BCM 和 GM。为了使膳食补充剂有希望减少食物来源的阿片肽的不良影响，必须支持在人体中使用 DPPIV 的体内研究。
