State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
Food Chem. 2022 Mar 15;372:131334. doi: 10.1016/j.foodchem.2021.131334. Epub 2021 Oct 5.
Due to the poor lipophilicity of chlorogenic acid (CA), five CA derivatives (C2-CA, C4-CA, C6-CA, C8-CA, and C12-CA) with different lipophilicities were synthesized using acylation catalyzed by lipase in present study. The inhibitory activities and mechanisms of CA and its derivatives on α-amylase and α-glucosidase were then determined. Results showed that the inhibitory activities of CA derivatives on α-amylase and α-glucosidase were enhanced as lipophilicity increased, and the inhibitory activities of C12-CA were stronger than those of CA. IC values of C12-CA were 13.30 ± 0.26 μmol/mL for α-amylase and 3.42 ± 0.10 μmol/mL for α-glucosidase. C12-CA possessed the smallest K and K values, and its inhibitory actions on α-amylase and α-glucosidase were stronger than those of CA and the other derivatives. Effects of C12-CA on microenvironments of amino acid residues and secondary structures of α-amylase and α-glucosidase were greater than those of CA and the other derivatives.
由于绿原酸（CA）的亲脂性较差，本研究采用脂肪酶催化酰化反应，合成了 5 种具有不同亲脂性的 CA 衍生物（C2-CA、C4-CA、C6-CA、C8-CA 和 C12-CA）。然后测定了 CA 及其衍生物对α-淀粉酶和α-葡萄糖苷酶的抑制活性和作用机制。结果表明，随着亲脂性的增加，CA 衍生物对α-淀粉酶和α-葡萄糖苷酶的抑制活性增强，C12-CA 的抑制活性强于 CA。C12-CA 对α-淀粉酶和α-葡萄糖苷酶的 IC 值分别为 13.30±0.26 μmol/mL 和 3.42±0.10 μmol/mL。C12-CA 的 K 和 K 值最小，对α-淀粉酶和α-葡萄糖苷酶的抑制作用强于 CA 和其他衍生物。C12-CA 对α-淀粉酶和α-葡萄糖苷酶的氨基酸残基微环境和二级结构的影响大于 CA 和其他衍生物。
