Sahnoun Mouna, Bejar Samir, Daoud Lobna, Ayadi Leila, Brini Faiçal, Saibi Walid
a Laboratory of Microbial Biotechnology and Engineering Enzymes (LMBEE), Centre of Biotechnology of Sfax (CBS) , University of Sfax , Sfax , Tunisia.
b Preparatory Institute for Engineering Studies, Sfax (IPEIS) , University of Sfax , Sfax , Tunisia.
Nat Prod Res. 2019 Mar;33(5):755-758. doi: 10.1080/14786419.2017.1408094. Epub 2017 Nov 28.
Among phenolic compounds, Agave americana L. extract contained puerarin (38.4%) and p-coumaric acid (12.29%) (pCa). From the Lineweaver-Burk plots, pCa and puerarin demonstrated a competitive and a non competitive inhibitions towards human α-amylase activity, respectively. PCa exhibited a higher human inhibitory activity with an IC of 98.8 μM which was about 2.3 times than acarbose. Puerarin (IC = 3.87 μM) and pCa (IC = 10.16 μM) also showed an excellent inhibition for Aspergillus oryzae S2 α-amylase activity. The inhibitions of the described biocatalysts compounds towards both amylases were significantly decreased when they were pre-incubated with starch. The binding modes of these compounds were evaluated in silico. The binding efficiency order of these molecules in terms of polar contact numbers for both enzymes was in agreement with the in vitro studies. These findings provided a rational reason to establish the isolated compounds capability as therapeutic target for hyperglycaemia modulation and antifungal therapy.
在酚类化合物中,龙舌兰提取物含有葛根素(38.4%)和对香豆酸(12.29%)(pCa)。从Lineweaver - Burk图来看,pCa和葛根素分别对人α -淀粉酶活性表现出竞争性抑制和非竞争性抑制。pCa对人的抑制活性更高,其IC50为98.8 μM,约为阿卡波糖的2.3倍。葛根素(IC50 = 3.87 μM)和pCa(IC50 = 10.16 μM)对米曲霉S2 α -淀粉酶活性也表现出优异的抑制作用。当这些生物催化剂化合物与淀粉预孵育时,它们对两种淀粉酶的抑制作用均显著降低。通过计算机模拟评估了这些化合物的结合模式。就两种酶的极性接触数而言,这些分子的结合效率顺序与体外研究一致。这些发现为确定分离出的化合物作为调节高血糖和抗真菌治疗的治疗靶点的能力提供了合理依据。