School of Biological Engineering, Dalian Polytechnic University, 1 Qinggongyuan, Dalian 116034, China.
Food Funct. 2020 May 1;11(5):4356-4362. doi: 10.1039/d0fo00625d. Epub 2020 May 5.
The flower of S. japonica is a favorite food and used as traditional medicine. In the present study, a facile and effective method based on the changes in the composition before and after the enzyme reaction was established to screen the active compounds from complex natural products. The separation of an active compound from the ethanolic extracts of Sophora japonica var. violacea, which exhibited the α-amylase inhibitory activity is presented as an example. The analysis of HPLC showed that one component was reduced by 25% after the enzyme reaction. The potential active compound was isolated via LH-20 gel permeation chromatography and identified as kaempferol 3-O-α-l-rhamnopyranosyl-(1 → 6)-β-d-galactopyranosyl-7-O-α-l-rhamnopyranoside by H and C NMR. The in vitro test indicated that the compound had the α-amylase inhibitory activity, and the IC was 88.56 ± 0.60 μg mL. The molecular docking study of this compound showed that the compound enfolded in the active sites of α-amylase completely and interacted with the amino acid residues through hydrogen bonds, van der Waals force and hydrophobic interactions.
山槐花是一种深受喜爱的食物，也被用作传统药物。在本研究中，建立了一种基于酶反应前后成分变化的简便、有效的方法，用于从复杂天然产物中筛选活性化合物。以从山槐醇提物中分离具有α-淀粉酶抑制活性的活性化合物为例。HPLC 分析表明，酶反应后有一个成分减少了 25%。通过 LH-20 凝胶渗透色谱分离得到潜在的活性化合物，并通过 1H 和 13C NMR 鉴定为山柰酚 3-O-α-l-鼠李吡喃糖基-(1 → 6)-β-d-半乳糖吡喃糖基-7-O-α-l-鼠李吡喃糖苷。体外试验表明，该化合物具有α-淀粉酶抑制活性，IC 为 88.56±0.60μg·mL-1。该化合物的分子对接研究表明，该化合物完全包裹在α-淀粉酶的活性部位，并通过氢键、范德华力和疏水相互作用与氨基酸残基相互作用。
