Iridoid glycosides from noni (Morinda citrifolia L.) fruit pomace: A novel booster strategy for its extraction and will its α-glucosidase inhibitory be increased by acetylation?
文献类型： 外文期刊
作者： Zhang, Chao 1 ; Gu, Chunhe 2 ; Su, Fan 2 ; Wang, Mengrui 1 ; Chen, Junxia 1 ; Chang, Ziqing 1 ; Zhou, Junping 1 ; Yue, Mingzhe 1 ; Liu, Fei 1 ; Feng, Zhen 2 ;
作者机构： 1.Northeast Agr Univ, Coll Food Sci, Key Lab Dairy Sci, Minist Educ, 600 Changjiang Rd, Harbin 150030, Heilongjiang, Peoples R China
2.Chinese Acad Trop Agr Sci, Spice & Beverage Res Inst, Wanning 571533, Hainan, Peoples R China
3.Key Lab Proc Suitabil & Qual Control Special Trop, Wanning 571533, Hainan, Peoples R China
关键词： Noni ( Morinda citrifolia L.) fruit pomace; Iridoid glycosides; Natural deep eutectic solvents; alpha-Glucosidase; Interaction mechanism
期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：6.6； 五年影响因子：6.9 ）
ISSN： 0023-6438
年卷期： 2024 年 207 卷
页码：
收录情况： SCI
摘要： Iridoid glycosides (IGs) are secondary metabolites found in plants such as the noni plant (Morinda citrifolia L.), known for their diverse biological activities and potential health benefits. Herein, we screened fifteen natural deep eutectic solvents (NADES) and two conventional solvents (CS, 70% (V/V) methanol and 70% (V/V) ethanol) for extraction of IGs from noni fruit pomace. Our findings indicate that non-acidic NADES promote IG extraction. Glycerol/glycine combined with (3-cyclodextrin was selected, and a molecular simulation was performed to elucidate the interaction between NADES components and IGs. Further, the structure-activity relationship and interaction mechanisms of IGs with alpha-glucosidase were investigated using multispectral and molecular docking tools. The results demonstrated that deacetylation of the B-ring's C-10 improved the inhibitory potential of IGs. Deacetylation produces hydrophobic contacts, which enhance the inhibitory effect of deacetylasperulosidic acid on alpha-glucosides. Additionally, hydrogen bonds and van der Waals forces drive the formation of non-covalent complexes between IGs and enzymes.
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