核桃（Juglans regia L.）蛋白来源的二肽基肽酶 IV 抑制肽的分离、鉴定及分子结合机制。
Separation, identification and molecular binding mechanism of dipeptidyl peptidase IV inhibitory peptides derived from walnut (Juglans regia L.) protein.
机构信息
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, PR China; School of Food Science and Technology, Jiangnan University, Wuxi, PR China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, PR China; School of Food Science and Technology, Jiangnan University, Wuxi, PR China.
出版信息
Food Chem. 2021 Jun 15;347:129062. doi: 10.1016/j.foodchem.2021.129062. Epub 2021 Jan 12.
Walnut protein was hydrolyzed with different proteases to evaluate the hydrolytic efficiency and dipeptidyl peptidase IV (DPP-IV) inhibitory activity in vitro. All of walnut protein hydrolysates (WPHs) exhibited DPP-IV inhibitory activity and Alcalase-derived hydrolysate (WPH-Alc) with better DPP-IV inhibitory activity of 33.90% (at 0.50 mg/mL) was subsequently separated by ultrafiltration and cation exchange chromatography on a SP Sephadex C-25 column. The results showed that fractions with lower molecular weight and higher basic amino acid residues possessed stronger DPP-IV inhibitory activity. Comparably, the obtained fraction B with the yield of 19.80% had the highest DPP-IV inhibitory activity of 76.19% at 0.25 mg/mL. Moreover, nine novel DPP-IV inhibitory peptides were identified using MALDI-TOF/TOF-MS. Molecular docking revealed the peptides could interact with DPP-IV through hydrogen bonds, salt bridges, hydrophobic interactions, π-cation bonds and π-π bonds. The walnut DPP-IV inhibitory peptides showed better stability with heating treatment, pH treatment, or in vitro gastrointestinal digestion.
采用不同蛋白酶水解山核桃蛋白，评价其体外酶解效率和二肽基肽酶 IV（DPP-IV）抑制活性。所有山核桃蛋白水解物（WPHs）均表现出 DPP-IV 抑制活性，其中碱性蛋白酶（Alcalase）衍生的水解物（WPH-Alc）的 DPP-IV 抑制活性最好，为 33.90%（在 0.50mg/mL 时），随后通过超滤和阳离子交换色谱 SP Sephadex C-25 柱进行分离。结果表明，具有较低分子量和较高碱性氨基酸残基的级分具有更强的 DPP-IV 抑制活性。相比之下，收率为 19.80%的获得级分 B 具有最高的 DPP-IV 抑制活性，为 76.19%（在 0.25mg/mL 时）。此外，使用 MALDI-TOF/TOF-MS 鉴定了 9 种新型 DPP-IV 抑制肽。分子对接表明，这些肽可以通过氢键、盐桥、疏水相互作用、π-阳离子键和 π-π 键与 DPP-IV 相互作用。山核桃 DPP-IV 抑制肽在热处理、pH 处理或体外胃肠消化过程中表现出更好的稳定性。
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