Zhejiang University, Department of Food Science and Nutrition, Zhejiang Key Laboratory for Agri-Food Processing, Fuli Institute of Food Science, Zhejiang R&D Centre for Food Technology and Equipment, Hangzhou 310058, China.
Zhejiang University, Department of Food Science and Nutrition, Zhejiang Key Laboratory for Agri-Food Processing, Fuli Institute of Food Science, Zhejiang R&D Centre for Food Technology and Equipment, Hangzhou 310058, China.
Food Chem. 2020 Jul 1;317:126346. doi: 10.1016/j.foodchem.2020.126346. Epub 2020 Feb 3.
The inhibitory mechanisms of ferulic acid against α-amylase and α-glucosidase were investigated by enzyme kinetic analysis, circular dichroism (CD), Fourier-transform infrared (FT-IR) spectroscopy, fluorescence quenching and molecular docking. Results indicated that ferulic acid strongly inhibited α-amylase (IC: 0.622 mg ml) and α-glucosidase (IC: 0.866 mg ml) by mixed and non-competitive mechanisms, respectively. CD spectra and fluorescence intensity measurements confirmed that the secondary structure of α-amylase and α-glucosidase were changed and the microenvironments of certain amino acid residues were modulated by the binding of ferulic acid. FT-IR spectra indicated that the interaction between ferulic acid and α-amylase/α-glucosidase mainly involved in non-covalent bonds. Molecular docking further demonstrated that the interaction forces between ferulic acid and α-amylase/α-glucosidase were hydrogen bonds, with the binding energy of -5.30 to -5.10 and -5.70 kcal mol, respectively. This study might provide a theoretical basis for the designing of novel functional foods with ferulic acid.
通过酶动力学分析、圆二色性（CD）、傅里叶变换红外（FT-IR）光谱、荧光猝灭和分子对接研究了阿魏酸对α-淀粉酶和α-葡萄糖苷酶的抑制机制。结果表明，阿魏酸通过混合和非竞争机制强烈抑制α-淀粉酶（IC：0.622 mg ml）和α-葡萄糖苷酶（IC：0.866 mg ml）。CD 光谱和荧光强度测量证实，阿魏酸的结合改变了α-淀粉酶和α-葡萄糖苷酶的二级结构，并调节了某些氨基酸残基的微环境。FT-IR 光谱表明，阿魏酸与α-淀粉酶/α-葡萄糖苷酶之间的相互作用主要涉及非共价键。分子对接进一步表明，阿魏酸与α-淀粉酶/α-葡萄糖苷酶之间的相互作用力为氢键，结合能分别为-5.30 至-5.10 和-5.70 kcal mol。本研究可为设计具有阿魏酸的新型功能性食品提供理论依据。
