Sahnoun Mouna, Saibi Walid, Brini Faiçal, Bejar Samir
1Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS), University of Sfax, Sidi Mansour Road Km 6, P.O. Box 1177, 3018 Sfax, Tunisia.
2Biotechnology and Plant Improvement Laboratory Centre of Biotechnology, Sfax University of Sfax, B.P 1177, 3018 Sfax, Tunisia.
J Food Sci Technol. 2018 Apr;55(4):1489-1498. doi: 10.1007/s13197-018-3065-6. Epub 2018 Feb 20.
extract was analyzed by reverse phase HPLC for characterization. Among phenolic compounds identified, apigenin was observed to be present. The finding showed an inhibitory effect of apigenin towards Human and S2 α-amylases. Apigenin inhibition towards Human and α-amylase activities was observed to be competitive. IC50 and % inhibition of apigenin for α-amylase were 3.98 and 1.65 fold higher than for Human α-amylase. The inhibition of the described biocatalyst activity was significantly lowered when apigenin was pre-incubated with starch. In addition to the catalytic residues, 44 amino acid residues were involved on α-amylase-apigenin interactions while only 11 amino acid residues were exposed for Human α-amylase-apigenin complex. The binding site of apigenin showed 76 polar contacts for S2 α-amylase against 44 interactions for Human α-amylase. The docking studies confirmed the mode of action of apigenin and strongly suggested a higher inhibitory activity towards fungal amylase which was experimentally exhibited. These findings provided a rational reason to establish apigenin capability as a therapeutic target for postprandial hyperglycaemia modulation and antifungal therapy.
提取物通过反相高效液相色谱法进行分析以进行表征。在所鉴定的酚类化合物中，观察到芹菜素的存在。该发现表明芹菜素对人源和S2α淀粉酶具有抑制作用。观察到芹菜素对人源α淀粉酶活性的抑制作用具有竞争性。芹菜素对α淀粉酶的IC50和抑制率比对人源α淀粉酶高3.98倍和1.65倍。当芹菜素与淀粉预孵育时，所述生物催化剂活性的抑制作用显著降低。除了催化残基外，44个氨基酸残基参与α淀粉酶与芹菜素的相互作用，而人源α淀粉酶与芹菜素复合物仅暴露11个氨基酸残基。芹菜素的结合位点显示与S2α淀粉酶有76个极性接触，而与人源α淀粉酶有44个相互作用。对接研究证实了芹菜素的作用模式，并强烈表明其对真菌淀粉酶具有更高的抑制活性，这在实验中得到了证实。这些发现为将芹菜素作为餐后高血糖调节和抗真菌治疗的治疗靶点的能力提供了合理依据。
